Unbound position II in MXCXXC metallochaperone model peptides impacts metal binding mode and reactivity: Distinct similarities to whole proteins
The effect of position II in the binding sequence of copper metallochaperones, which varies between Thr and His, was investigated through structural analysis and affinity and oxidation kinetic studies of model peptides. A first Cys–Cu(I)–Cys model obtained for the His peptide at acidic and neutral p...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Shoshan, Michal S. [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2016transfer abstract |
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| Umfang: |
8 |
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| Übergeordnetes Werk: |
Enthalten in: Severe Staphylococcus aureus infection and melanoma risk: A large single center observational cohort study - 2015, an interdisciplinary journal, New York, NY [u.a.] |
|---|---|
| Übergeordnetes Werk: |
volume:159 ; year:2016 ; pages:29-36 ; extent:8 |
| Links: |
|---|
| DOI / URN: |
10.1016/j.jinorgbio.2016.02.016 |
|---|
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ELV029525446 |
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| 245 | 1 | 0 | |a Unbound position II in MXCXXC metallochaperone model peptides impacts metal binding mode and reactivity: Distinct similarities to whole proteins |
| 264 | 1 | |c 2016transfer abstract | |
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| 520 | |a The effect of position II in the binding sequence of copper metallochaperones, which varies between Thr and His, was investigated through structural analysis and affinity and oxidation kinetic studies of model peptides. A first Cys–Cu(I)–Cys model obtained for the His peptide at acidic and neutral pH, correlated with higher affinity and more rapid oxidation of its complex; in contrast, the Thr peptide with the Cys–Cu(I)–Met coordination under neutral conditions demonstrated weaker and pH dependent binding. Studies with human antioxidant protein 1 (Atox1) and three of its mutants where S residues were replaced with Ala suggested that (a) the binding affinity is influenced more by the binding sequence than by the protein fold (b) pH may play a role in binding reactivity, and (c) mutating the Met impacted the affinity and oxidation rate more drastically than did mutating one of the Cys, supporting its important role in protein function. Position II thus plays a dominant role in metal binding and transport. | ||
| 520 | |a The effect of position II in the binding sequence of copper metallochaperones, which varies between Thr and His, was investigated through structural analysis and affinity and oxidation kinetic studies of model peptides. A first Cys–Cu(I)–Cys model obtained for the His peptide at acidic and neutral pH, correlated with higher affinity and more rapid oxidation of its complex; in contrast, the Thr peptide with the Cys–Cu(I)–Met coordination under neutral conditions demonstrated weaker and pH dependent binding. Studies with human antioxidant protein 1 (Atox1) and three of its mutants where S residues were replaced with Ala suggested that (a) the binding affinity is influenced more by the binding sequence than by the protein fold (b) pH may play a role in binding reactivity, and (c) mutating the Met impacted the affinity and oxidation rate more drastically than did mutating one of the Cys, supporting its important role in protein function. Position II thus plays a dominant role in metal binding and transport. | ||
| 700 | 1 | |a Dekel, Noa |4 oth | |
| 700 | 1 | |a Goch, Wojciech |4 oth | |
| 700 | 1 | |a Shalev, Deborah E. |4 oth | |
| 700 | 1 | |a Danieli, Tsafi |4 oth | |
| 700 | 1 | |a Lebendiker, Mario |4 oth | |
| 700 | 1 | |a Bal, Wojciech |4 oth | |
| 700 | 1 | |a Tshuva, Edit Y. |4 oth | |
| 773 | 0 | 8 | |i Enthalten in |n Elsevier |t Severe Staphylococcus aureus infection and melanoma risk: A large single center observational cohort study |d 2015 |d an interdisciplinary journal |g New York, NY [u.a.] |w (DE-627)ELV018319009 |
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10.1016/j.jinorgbio.2016.02.016 doi GBVA2016004000011.pica (DE-627)ELV029525446 (ELSEVIER)S0162-0134(16)30041-1 DE-627 ger DE-627 rakwb eng 540 540 DE-600 610 VZ 333.7 610 VZ 43.12 bkl 43.13 bkl 44.13 bkl Shoshan, Michal S. verfasserin aut Unbound position II in MXCXXC metallochaperone model peptides impacts metal binding mode and reactivity: Distinct similarities to whole proteins 2016transfer abstract 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The effect of position II in the binding sequence of copper metallochaperones, which varies between Thr and His, was investigated through structural analysis and affinity and oxidation kinetic studies of model peptides. A first Cys–Cu(I)–Cys model obtained for the His peptide at acidic and neutral pH, correlated with higher affinity and more rapid oxidation of its complex; in contrast, the Thr peptide with the Cys–Cu(I)–Met coordination under neutral conditions demonstrated weaker and pH dependent binding. Studies with human antioxidant protein 1 (Atox1) and three of its mutants where S residues were replaced with Ala suggested that (a) the binding affinity is influenced more by the binding sequence than by the protein fold (b) pH may play a role in binding reactivity, and (c) mutating the Met impacted the affinity and oxidation rate more drastically than did mutating one of the Cys, supporting its important role in protein function. Position II thus plays a dominant role in metal binding and transport. The effect of position II in the binding sequence of copper metallochaperones, which varies between Thr and His, was investigated through structural analysis and affinity and oxidation kinetic studies of model peptides. A first Cys–Cu(I)–Cys model obtained for the His peptide at acidic and neutral pH, correlated with higher affinity and more rapid oxidation of its complex; in contrast, the Thr peptide with the Cys–Cu(I)–Met coordination under neutral conditions demonstrated weaker and pH dependent binding. Studies with human antioxidant protein 1 (Atox1) and three of its mutants where S residues were replaced with Ala suggested that (a) the binding affinity is influenced more by the binding sequence than by the protein fold (b) pH may play a role in binding reactivity, and (c) mutating the Met impacted the affinity and oxidation rate more drastically than did mutating one of the Cys, supporting its important role in protein function. Position II thus plays a dominant role in metal binding and transport. Dekel, Noa oth Goch, Wojciech oth Shalev, Deborah E. oth Danieli, Tsafi oth Lebendiker, Mario oth Bal, Wojciech oth Tshuva, Edit Y. oth Enthalten in Elsevier Severe Staphylococcus aureus infection and melanoma risk: A large single center observational cohort study 2015 an interdisciplinary journal New York, NY [u.a.] (DE-627)ELV018319009 volume:159 year:2016 pages:29-36 extent:8 https://doi.org/10.1016/j.jinorgbio.2016.02.016 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA SSG-OPC-GGO GBV_ILN_40 43.12 Umweltchemie VZ 43.13 Umwelttoxikologie VZ 44.13 Medizinische Ökologie VZ AR 159 2016 29-36 8 045F 540 |
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10.1016/j.jinorgbio.2016.02.016 doi GBVA2016004000011.pica (DE-627)ELV029525446 (ELSEVIER)S0162-0134(16)30041-1 DE-627 ger DE-627 rakwb eng 540 540 DE-600 610 VZ 333.7 610 VZ 43.12 bkl 43.13 bkl 44.13 bkl Shoshan, Michal S. verfasserin aut Unbound position II in MXCXXC metallochaperone model peptides impacts metal binding mode and reactivity: Distinct similarities to whole proteins 2016transfer abstract 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The effect of position II in the binding sequence of copper metallochaperones, which varies between Thr and His, was investigated through structural analysis and affinity and oxidation kinetic studies of model peptides. A first Cys–Cu(I)–Cys model obtained for the His peptide at acidic and neutral pH, correlated with higher affinity and more rapid oxidation of its complex; in contrast, the Thr peptide with the Cys–Cu(I)–Met coordination under neutral conditions demonstrated weaker and pH dependent binding. Studies with human antioxidant protein 1 (Atox1) and three of its mutants where S residues were replaced with Ala suggested that (a) the binding affinity is influenced more by the binding sequence than by the protein fold (b) pH may play a role in binding reactivity, and (c) mutating the Met impacted the affinity and oxidation rate more drastically than did mutating one of the Cys, supporting its important role in protein function. Position II thus plays a dominant role in metal binding and transport. The effect of position II in the binding sequence of copper metallochaperones, which varies between Thr and His, was investigated through structural analysis and affinity and oxidation kinetic studies of model peptides. A first Cys–Cu(I)–Cys model obtained for the His peptide at acidic and neutral pH, correlated with higher affinity and more rapid oxidation of its complex; in contrast, the Thr peptide with the Cys–Cu(I)–Met coordination under neutral conditions demonstrated weaker and pH dependent binding. Studies with human antioxidant protein 1 (Atox1) and three of its mutants where S residues were replaced with Ala suggested that (a) the binding affinity is influenced more by the binding sequence than by the protein fold (b) pH may play a role in binding reactivity, and (c) mutating the Met impacted the affinity and oxidation rate more drastically than did mutating one of the Cys, supporting its important role in protein function. Position II thus plays a dominant role in metal binding and transport. Dekel, Noa oth Goch, Wojciech oth Shalev, Deborah E. oth Danieli, Tsafi oth Lebendiker, Mario oth Bal, Wojciech oth Tshuva, Edit Y. oth Enthalten in Elsevier Severe Staphylococcus aureus infection and melanoma risk: A large single center observational cohort study 2015 an interdisciplinary journal New York, NY [u.a.] (DE-627)ELV018319009 volume:159 year:2016 pages:29-36 extent:8 https://doi.org/10.1016/j.jinorgbio.2016.02.016 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA SSG-OPC-GGO GBV_ILN_40 43.12 Umweltchemie VZ 43.13 Umwelttoxikologie VZ 44.13 Medizinische Ökologie VZ AR 159 2016 29-36 8 045F 540 |
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10.1016/j.jinorgbio.2016.02.016 doi GBVA2016004000011.pica (DE-627)ELV029525446 (ELSEVIER)S0162-0134(16)30041-1 DE-627 ger DE-627 rakwb eng 540 540 DE-600 610 VZ 333.7 610 VZ 43.12 bkl 43.13 bkl 44.13 bkl Shoshan, Michal S. verfasserin aut Unbound position II in MXCXXC metallochaperone model peptides impacts metal binding mode and reactivity: Distinct similarities to whole proteins 2016transfer abstract 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The effect of position II in the binding sequence of copper metallochaperones, which varies between Thr and His, was investigated through structural analysis and affinity and oxidation kinetic studies of model peptides. A first Cys–Cu(I)–Cys model obtained for the His peptide at acidic and neutral pH, correlated with higher affinity and more rapid oxidation of its complex; in contrast, the Thr peptide with the Cys–Cu(I)–Met coordination under neutral conditions demonstrated weaker and pH dependent binding. Studies with human antioxidant protein 1 (Atox1) and three of its mutants where S residues were replaced with Ala suggested that (a) the binding affinity is influenced more by the binding sequence than by the protein fold (b) pH may play a role in binding reactivity, and (c) mutating the Met impacted the affinity and oxidation rate more drastically than did mutating one of the Cys, supporting its important role in protein function. Position II thus plays a dominant role in metal binding and transport. The effect of position II in the binding sequence of copper metallochaperones, which varies between Thr and His, was investigated through structural analysis and affinity and oxidation kinetic studies of model peptides. A first Cys–Cu(I)–Cys model obtained for the His peptide at acidic and neutral pH, correlated with higher affinity and more rapid oxidation of its complex; in contrast, the Thr peptide with the Cys–Cu(I)–Met coordination under neutral conditions demonstrated weaker and pH dependent binding. Studies with human antioxidant protein 1 (Atox1) and three of its mutants where S residues were replaced with Ala suggested that (a) the binding affinity is influenced more by the binding sequence than by the protein fold (b) pH may play a role in binding reactivity, and (c) mutating the Met impacted the affinity and oxidation rate more drastically than did mutating one of the Cys, supporting its important role in protein function. Position II thus plays a dominant role in metal binding and transport. Dekel, Noa oth Goch, Wojciech oth Shalev, Deborah E. oth Danieli, Tsafi oth Lebendiker, Mario oth Bal, Wojciech oth Tshuva, Edit Y. oth Enthalten in Elsevier Severe Staphylococcus aureus infection and melanoma risk: A large single center observational cohort study 2015 an interdisciplinary journal New York, NY [u.a.] (DE-627)ELV018319009 volume:159 year:2016 pages:29-36 extent:8 https://doi.org/10.1016/j.jinorgbio.2016.02.016 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA SSG-OPC-GGO GBV_ILN_40 43.12 Umweltchemie VZ 43.13 Umwelttoxikologie VZ 44.13 Medizinische Ökologie VZ AR 159 2016 29-36 8 045F 540 |
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10.1016/j.jinorgbio.2016.02.016 doi GBVA2016004000011.pica (DE-627)ELV029525446 (ELSEVIER)S0162-0134(16)30041-1 DE-627 ger DE-627 rakwb eng 540 540 DE-600 610 VZ 333.7 610 VZ 43.12 bkl 43.13 bkl 44.13 bkl Shoshan, Michal S. verfasserin aut Unbound position II in MXCXXC metallochaperone model peptides impacts metal binding mode and reactivity: Distinct similarities to whole proteins 2016transfer abstract 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The effect of position II in the binding sequence of copper metallochaperones, which varies between Thr and His, was investigated through structural analysis and affinity and oxidation kinetic studies of model peptides. A first Cys–Cu(I)–Cys model obtained for the His peptide at acidic and neutral pH, correlated with higher affinity and more rapid oxidation of its complex; in contrast, the Thr peptide with the Cys–Cu(I)–Met coordination under neutral conditions demonstrated weaker and pH dependent binding. Studies with human antioxidant protein 1 (Atox1) and three of its mutants where S residues were replaced with Ala suggested that (a) the binding affinity is influenced more by the binding sequence than by the protein fold (b) pH may play a role in binding reactivity, and (c) mutating the Met impacted the affinity and oxidation rate more drastically than did mutating one of the Cys, supporting its important role in protein function. Position II thus plays a dominant role in metal binding and transport. The effect of position II in the binding sequence of copper metallochaperones, which varies between Thr and His, was investigated through structural analysis and affinity and oxidation kinetic studies of model peptides. A first Cys–Cu(I)–Cys model obtained for the His peptide at acidic and neutral pH, correlated with higher affinity and more rapid oxidation of its complex; in contrast, the Thr peptide with the Cys–Cu(I)–Met coordination under neutral conditions demonstrated weaker and pH dependent binding. Studies with human antioxidant protein 1 (Atox1) and three of its mutants where S residues were replaced with Ala suggested that (a) the binding affinity is influenced more by the binding sequence than by the protein fold (b) pH may play a role in binding reactivity, and (c) mutating the Met impacted the affinity and oxidation rate more drastically than did mutating one of the Cys, supporting its important role in protein function. Position II thus plays a dominant role in metal binding and transport. Dekel, Noa oth Goch, Wojciech oth Shalev, Deborah E. oth Danieli, Tsafi oth Lebendiker, Mario oth Bal, Wojciech oth Tshuva, Edit Y. oth Enthalten in Elsevier Severe Staphylococcus aureus infection and melanoma risk: A large single center observational cohort study 2015 an interdisciplinary journal New York, NY [u.a.] (DE-627)ELV018319009 volume:159 year:2016 pages:29-36 extent:8 https://doi.org/10.1016/j.jinorgbio.2016.02.016 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA SSG-OPC-GGO GBV_ILN_40 43.12 Umweltchemie VZ 43.13 Umwelttoxikologie VZ 44.13 Medizinische Ökologie VZ AR 159 2016 29-36 8 045F 540 |
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10.1016/j.jinorgbio.2016.02.016 doi GBVA2016004000011.pica (DE-627)ELV029525446 (ELSEVIER)S0162-0134(16)30041-1 DE-627 ger DE-627 rakwb eng 540 540 DE-600 610 VZ 333.7 610 VZ 43.12 bkl 43.13 bkl 44.13 bkl Shoshan, Michal S. verfasserin aut Unbound position II in MXCXXC metallochaperone model peptides impacts metal binding mode and reactivity: Distinct similarities to whole proteins 2016transfer abstract 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The effect of position II in the binding sequence of copper metallochaperones, which varies between Thr and His, was investigated through structural analysis and affinity and oxidation kinetic studies of model peptides. A first Cys–Cu(I)–Cys model obtained for the His peptide at acidic and neutral pH, correlated with higher affinity and more rapid oxidation of its complex; in contrast, the Thr peptide with the Cys–Cu(I)–Met coordination under neutral conditions demonstrated weaker and pH dependent binding. Studies with human antioxidant protein 1 (Atox1) and three of its mutants where S residues were replaced with Ala suggested that (a) the binding affinity is influenced more by the binding sequence than by the protein fold (b) pH may play a role in binding reactivity, and (c) mutating the Met impacted the affinity and oxidation rate more drastically than did mutating one of the Cys, supporting its important role in protein function. Position II thus plays a dominant role in metal binding and transport. The effect of position II in the binding sequence of copper metallochaperones, which varies between Thr and His, was investigated through structural analysis and affinity and oxidation kinetic studies of model peptides. A first Cys–Cu(I)–Cys model obtained for the His peptide at acidic and neutral pH, correlated with higher affinity and more rapid oxidation of its complex; in contrast, the Thr peptide with the Cys–Cu(I)–Met coordination under neutral conditions demonstrated weaker and pH dependent binding. Studies with human antioxidant protein 1 (Atox1) and three of its mutants where S residues were replaced with Ala suggested that (a) the binding affinity is influenced more by the binding sequence than by the protein fold (b) pH may play a role in binding reactivity, and (c) mutating the Met impacted the affinity and oxidation rate more drastically than did mutating one of the Cys, supporting its important role in protein function. Position II thus plays a dominant role in metal binding and transport. Dekel, Noa oth Goch, Wojciech oth Shalev, Deborah E. oth Danieli, Tsafi oth Lebendiker, Mario oth Bal, Wojciech oth Tshuva, Edit Y. oth Enthalten in Elsevier Severe Staphylococcus aureus infection and melanoma risk: A large single center observational cohort study 2015 an interdisciplinary journal New York, NY [u.a.] (DE-627)ELV018319009 volume:159 year:2016 pages:29-36 extent:8 https://doi.org/10.1016/j.jinorgbio.2016.02.016 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA SSG-OPC-GGO GBV_ILN_40 43.12 Umweltchemie VZ 43.13 Umwelttoxikologie VZ 44.13 Medizinische Ökologie VZ AR 159 2016 29-36 8 045F 540 |
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Enthalten in Severe Staphylococcus aureus infection and melanoma risk: A large single center observational cohort study New York, NY [u.a.] volume:159 year:2016 pages:29-36 extent:8 |
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Enthalten in Severe Staphylococcus aureus infection and melanoma risk: A large single center observational cohort study New York, NY [u.a.] volume:159 year:2016 pages:29-36 extent:8 |
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Severe Staphylococcus aureus infection and melanoma risk: A large single center observational cohort study |
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unbound position ii in mxcxxc metallochaperone model peptides impacts metal binding mode and reactivity: distinct similarities to whole proteins |
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Unbound position II in MXCXXC metallochaperone model peptides impacts metal binding mode and reactivity: Distinct similarities to whole proteins |
| abstract |
The effect of position II in the binding sequence of copper metallochaperones, which varies between Thr and His, was investigated through structural analysis and affinity and oxidation kinetic studies of model peptides. A first Cys–Cu(I)–Cys model obtained for the His peptide at acidic and neutral pH, correlated with higher affinity and more rapid oxidation of its complex; in contrast, the Thr peptide with the Cys–Cu(I)–Met coordination under neutral conditions demonstrated weaker and pH dependent binding. Studies with human antioxidant protein 1 (Atox1) and three of its mutants where S residues were replaced with Ala suggested that (a) the binding affinity is influenced more by the binding sequence than by the protein fold (b) pH may play a role in binding reactivity, and (c) mutating the Met impacted the affinity and oxidation rate more drastically than did mutating one of the Cys, supporting its important role in protein function. Position II thus plays a dominant role in metal binding and transport. |
| abstractGer |
The effect of position II in the binding sequence of copper metallochaperones, which varies between Thr and His, was investigated through structural analysis and affinity and oxidation kinetic studies of model peptides. A first Cys–Cu(I)–Cys model obtained for the His peptide at acidic and neutral pH, correlated with higher affinity and more rapid oxidation of its complex; in contrast, the Thr peptide with the Cys–Cu(I)–Met coordination under neutral conditions demonstrated weaker and pH dependent binding. Studies with human antioxidant protein 1 (Atox1) and three of its mutants where S residues were replaced with Ala suggested that (a) the binding affinity is influenced more by the binding sequence than by the protein fold (b) pH may play a role in binding reactivity, and (c) mutating the Met impacted the affinity and oxidation rate more drastically than did mutating one of the Cys, supporting its important role in protein function. Position II thus plays a dominant role in metal binding and transport. |
| abstract_unstemmed |
The effect of position II in the binding sequence of copper metallochaperones, which varies between Thr and His, was investigated through structural analysis and affinity and oxidation kinetic studies of model peptides. A first Cys–Cu(I)–Cys model obtained for the His peptide at acidic and neutral pH, correlated with higher affinity and more rapid oxidation of its complex; in contrast, the Thr peptide with the Cys–Cu(I)–Met coordination under neutral conditions demonstrated weaker and pH dependent binding. Studies with human antioxidant protein 1 (Atox1) and three of its mutants where S residues were replaced with Ala suggested that (a) the binding affinity is influenced more by the binding sequence than by the protein fold (b) pH may play a role in binding reactivity, and (c) mutating the Met impacted the affinity and oxidation rate more drastically than did mutating one of the Cys, supporting its important role in protein function. Position II thus plays a dominant role in metal binding and transport. |
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Unbound position II in MXCXXC metallochaperone model peptides impacts metal binding mode and reactivity: Distinct similarities to whole proteins |
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