In various protein complexes, disordered protomers have large per‐residue surface areas and area of protein‐, DNA‐ and RNA‐binding interfaces
We provide first large scale analysis of the peculiarities of surface areas of 5658 dissimilar (below 50% sequence similarity) proteins with known 3D‐structures that bind to proteins, DNA or RNAs. We show here that area of the protein surface is highly correlated with the protein length. The size of...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Wu, Zhonghua [verfasserIn] |
|---|
| Format: |
Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2015 |
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| Rechteinformationen: |
Nutzungsrecht: FEBS Letters 589 (2015) 1873-3468 © 2015 Federation of European Biochemical Societies Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. |
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| Schlagwörter: |
Intrinsically Disordered Proteins - metabolism Computational Biology - methods Intrinsically Disordered Proteins - chemistry Multiprotein Complexes - metabolism |
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| Übergeordnetes Werk: |
Enthalten in: FEBS letters - Amsterdam [u.a.] : Elsevier, 1968, 589(2015), 19PartA, Seite 2561-2569 |
|---|---|
| Übergeordnetes Werk: |
volume:589 ; year:2015 ; number:19PartA ; pages:2561-2569 |
| Links: |
|---|
| DOI / URN: |
10.1016/j.febslet.2015.08.014 |
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| 245 | 1 | 0 | |a In various protein complexes, disordered protomers have large per‐residue surface areas and area of protein‐, DNA‐ and RNA‐binding interfaces |
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| 520 | |a We provide first large scale analysis of the peculiarities of surface areas of 5658 dissimilar (below 50% sequence similarity) proteins with known 3D‐structures that bind to proteins, DNA or RNAs. We show here that area of the protein surface is highly correlated with the protein length. The size of the interface surface is only modestly correlated with the protein size, except for RNA‐binding proteins where larger proteins are characterized by larger interfaces. Disordered proteins with disordered interfaces are characterized by significantly larger per‐residue areas of their surfaces and interfaces when compared to the structured proteins. These result are applicable for proteins involved in interaction with DNA, RNA, and proteins and suggest that disordered proteins and binding regions are less compact and more likely to assume extended shape. We demonstrate that disordered protein binding residues in the interfaces of disordered proteins drive the increase in the per residue area of these interfaces. Our results can be used to predict in silico whether a given protomer from the DNA, RNA or protein complex is likely to be disordered in its unbound form. | ||
| 540 | |a Nutzungsrecht: FEBS Letters 589 (2015) 1873-3468 © 2015 Federation of European Biochemical Societies | ||
| 540 | |a Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. | ||
| 650 | 4 | |a Protein–protein interaction | |
| 650 | 4 | |a Protein–DNA interaction | |
| 650 | 4 | |a Protein–RNA interaction | |
| 650 | 4 | |a Binding interface | |
| 650 | 4 | |a Intrinsic disorder | |
| 650 | 4 | |a Binding surface | |
| 650 | 4 | |a Intrinsically Disordered Proteins - metabolism | |
| 650 | 4 | |a RNA - metabolism | |
| 650 | 4 | |a Computational Biology - methods | |
| 650 | 4 | |a Intrinsically Disordered Proteins - chemistry | |
| 650 | 4 | |a DNA - metabolism | |
| 650 | 4 | |a Multiprotein Complexes - metabolism | |
| 650 | 4 | |a Multiprotein Complexes - chemistry | |
| 650 | 4 | |a RNA - chemistry | |
| 650 | 4 | |a DNA - chemistry | |
| 700 | 1 | |a Hu, Gang |4 oth | |
| 700 | 1 | |a Yang, Jianyi |4 oth | |
| 700 | 1 | |a Peng, Zhenling |4 oth | |
| 700 | 1 | |a Uversky, Vladimir N |4 oth | |
| 700 | 1 | |a Kurgan, Lukasz |4 oth | |
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10.1016/j.febslet.2015.08.014 doi PQ20160617 (DE-627)OLC196554777X (DE-599)GBVOLC196554777X (PRQ)c2239-eb44a43fd072197cb5e5f4eb05b59d838e3e966129421358cdb755d870307e610 (KEY)0045922420150000589001902561invariousproteincomplexesdisorderedprotomershavela DE-627 ger DE-627 rakwb eng 570 530 610 DNB Wu, Zhonghua verfasserin aut In various protein complexes, disordered protomers have large per‐residue surface areas and area of protein‐, DNA‐ and RNA‐binding interfaces 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier We provide first large scale analysis of the peculiarities of surface areas of 5658 dissimilar (below 50% sequence similarity) proteins with known 3D‐structures that bind to proteins, DNA or RNAs. We show here that area of the protein surface is highly correlated with the protein length. The size of the interface surface is only modestly correlated with the protein size, except for RNA‐binding proteins where larger proteins are characterized by larger interfaces. Disordered proteins with disordered interfaces are characterized by significantly larger per‐residue areas of their surfaces and interfaces when compared to the structured proteins. These result are applicable for proteins involved in interaction with DNA, RNA, and proteins and suggest that disordered proteins and binding regions are less compact and more likely to assume extended shape. We demonstrate that disordered protein binding residues in the interfaces of disordered proteins drive the increase in the per residue area of these interfaces. Our results can be used to predict in silico whether a given protomer from the DNA, RNA or protein complex is likely to be disordered in its unbound form. Nutzungsrecht: FEBS Letters 589 (2015) 1873-3468 © 2015 Federation of European Biochemical Societies Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. Protein–protein interaction Protein–DNA interaction Protein–RNA interaction Binding interface Intrinsic disorder Binding surface Intrinsically Disordered Proteins - metabolism RNA - metabolism Computational Biology - methods Intrinsically Disordered Proteins - chemistry DNA - metabolism Multiprotein Complexes - metabolism Multiprotein Complexes - chemistry RNA - chemistry DNA - chemistry Hu, Gang oth Yang, Jianyi oth Peng, Zhenling oth Uversky, Vladimir N oth Kurgan, Lukasz oth Enthalten in FEBS letters Amsterdam [u.a.] : Elsevier, 1968 589(2015), 19PartA, Seite 2561-2569 (DE-627)129522023 (DE-600)212746-5 (DE-576)014938014 0014-5793 nnns volume:589 year:2015 number:19PartA pages:2561-2569 http://dx.doi.org/10.1016/j.febslet.2015.08.014 Volltext http://onlinelibrary.wiley.com/doi/10.1016/j.febslet.2015.08.014/abstract http://www.ncbi.nlm.nih.gov/pubmed/26297830 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_21 GBV_ILN_70 GBV_ILN_211 GBV_ILN_2219 GBV_ILN_4012 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4305 AR 589 2015 19PartA 2561-2569 |
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10.1016/j.febslet.2015.08.014 doi PQ20160617 (DE-627)OLC196554777X (DE-599)GBVOLC196554777X (PRQ)c2239-eb44a43fd072197cb5e5f4eb05b59d838e3e966129421358cdb755d870307e610 (KEY)0045922420150000589001902561invariousproteincomplexesdisorderedprotomershavela DE-627 ger DE-627 rakwb eng 570 530 610 DNB Wu, Zhonghua verfasserin aut In various protein complexes, disordered protomers have large per‐residue surface areas and area of protein‐, DNA‐ and RNA‐binding interfaces 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier We provide first large scale analysis of the peculiarities of surface areas of 5658 dissimilar (below 50% sequence similarity) proteins with known 3D‐structures that bind to proteins, DNA or RNAs. We show here that area of the protein surface is highly correlated with the protein length. The size of the interface surface is only modestly correlated with the protein size, except for RNA‐binding proteins where larger proteins are characterized by larger interfaces. Disordered proteins with disordered interfaces are characterized by significantly larger per‐residue areas of their surfaces and interfaces when compared to the structured proteins. These result are applicable for proteins involved in interaction with DNA, RNA, and proteins and suggest that disordered proteins and binding regions are less compact and more likely to assume extended shape. We demonstrate that disordered protein binding residues in the interfaces of disordered proteins drive the increase in the per residue area of these interfaces. Our results can be used to predict in silico whether a given protomer from the DNA, RNA or protein complex is likely to be disordered in its unbound form. Nutzungsrecht: FEBS Letters 589 (2015) 1873-3468 © 2015 Federation of European Biochemical Societies Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. Protein–protein interaction Protein–DNA interaction Protein–RNA interaction Binding interface Intrinsic disorder Binding surface Intrinsically Disordered Proteins - metabolism RNA - metabolism Computational Biology - methods Intrinsically Disordered Proteins - chemistry DNA - metabolism Multiprotein Complexes - metabolism Multiprotein Complexes - chemistry RNA - chemistry DNA - chemistry Hu, Gang oth Yang, Jianyi oth Peng, Zhenling oth Uversky, Vladimir N oth Kurgan, Lukasz oth Enthalten in FEBS letters Amsterdam [u.a.] : Elsevier, 1968 589(2015), 19PartA, Seite 2561-2569 (DE-627)129522023 (DE-600)212746-5 (DE-576)014938014 0014-5793 nnns volume:589 year:2015 number:19PartA pages:2561-2569 http://dx.doi.org/10.1016/j.febslet.2015.08.014 Volltext http://onlinelibrary.wiley.com/doi/10.1016/j.febslet.2015.08.014/abstract http://www.ncbi.nlm.nih.gov/pubmed/26297830 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_21 GBV_ILN_70 GBV_ILN_211 GBV_ILN_2219 GBV_ILN_4012 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4305 AR 589 2015 19PartA 2561-2569 |
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10.1016/j.febslet.2015.08.014 doi PQ20160617 (DE-627)OLC196554777X (DE-599)GBVOLC196554777X (PRQ)c2239-eb44a43fd072197cb5e5f4eb05b59d838e3e966129421358cdb755d870307e610 (KEY)0045922420150000589001902561invariousproteincomplexesdisorderedprotomershavela DE-627 ger DE-627 rakwb eng 570 530 610 DNB Wu, Zhonghua verfasserin aut In various protein complexes, disordered protomers have large per‐residue surface areas and area of protein‐, DNA‐ and RNA‐binding interfaces 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier We provide first large scale analysis of the peculiarities of surface areas of 5658 dissimilar (below 50% sequence similarity) proteins with known 3D‐structures that bind to proteins, DNA or RNAs. We show here that area of the protein surface is highly correlated with the protein length. The size of the interface surface is only modestly correlated with the protein size, except for RNA‐binding proteins where larger proteins are characterized by larger interfaces. Disordered proteins with disordered interfaces are characterized by significantly larger per‐residue areas of their surfaces and interfaces when compared to the structured proteins. These result are applicable for proteins involved in interaction with DNA, RNA, and proteins and suggest that disordered proteins and binding regions are less compact and more likely to assume extended shape. We demonstrate that disordered protein binding residues in the interfaces of disordered proteins drive the increase in the per residue area of these interfaces. Our results can be used to predict in silico whether a given protomer from the DNA, RNA or protein complex is likely to be disordered in its unbound form. Nutzungsrecht: FEBS Letters 589 (2015) 1873-3468 © 2015 Federation of European Biochemical Societies Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. Protein–protein interaction Protein–DNA interaction Protein–RNA interaction Binding interface Intrinsic disorder Binding surface Intrinsically Disordered Proteins - metabolism RNA - metabolism Computational Biology - methods Intrinsically Disordered Proteins - chemistry DNA - metabolism Multiprotein Complexes - metabolism Multiprotein Complexes - chemistry RNA - chemistry DNA - chemistry Hu, Gang oth Yang, Jianyi oth Peng, Zhenling oth Uversky, Vladimir N oth Kurgan, Lukasz oth Enthalten in FEBS letters Amsterdam [u.a.] : Elsevier, 1968 589(2015), 19PartA, Seite 2561-2569 (DE-627)129522023 (DE-600)212746-5 (DE-576)014938014 0014-5793 nnns volume:589 year:2015 number:19PartA pages:2561-2569 http://dx.doi.org/10.1016/j.febslet.2015.08.014 Volltext http://onlinelibrary.wiley.com/doi/10.1016/j.febslet.2015.08.014/abstract http://www.ncbi.nlm.nih.gov/pubmed/26297830 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_21 GBV_ILN_70 GBV_ILN_211 GBV_ILN_2219 GBV_ILN_4012 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4305 AR 589 2015 19PartA 2561-2569 |
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10.1016/j.febslet.2015.08.014 doi PQ20160617 (DE-627)OLC196554777X (DE-599)GBVOLC196554777X (PRQ)c2239-eb44a43fd072197cb5e5f4eb05b59d838e3e966129421358cdb755d870307e610 (KEY)0045922420150000589001902561invariousproteincomplexesdisorderedprotomershavela DE-627 ger DE-627 rakwb eng 570 530 610 DNB Wu, Zhonghua verfasserin aut In various protein complexes, disordered protomers have large per‐residue surface areas and area of protein‐, DNA‐ and RNA‐binding interfaces 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier We provide first large scale analysis of the peculiarities of surface areas of 5658 dissimilar (below 50% sequence similarity) proteins with known 3D‐structures that bind to proteins, DNA or RNAs. We show here that area of the protein surface is highly correlated with the protein length. The size of the interface surface is only modestly correlated with the protein size, except for RNA‐binding proteins where larger proteins are characterized by larger interfaces. Disordered proteins with disordered interfaces are characterized by significantly larger per‐residue areas of their surfaces and interfaces when compared to the structured proteins. These result are applicable for proteins involved in interaction with DNA, RNA, and proteins and suggest that disordered proteins and binding regions are less compact and more likely to assume extended shape. We demonstrate that disordered protein binding residues in the interfaces of disordered proteins drive the increase in the per residue area of these interfaces. Our results can be used to predict in silico whether a given protomer from the DNA, RNA or protein complex is likely to be disordered in its unbound form. Nutzungsrecht: FEBS Letters 589 (2015) 1873-3468 © 2015 Federation of European Biochemical Societies Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. Protein–protein interaction Protein–DNA interaction Protein–RNA interaction Binding interface Intrinsic disorder Binding surface Intrinsically Disordered Proteins - metabolism RNA - metabolism Computational Biology - methods Intrinsically Disordered Proteins - chemistry DNA - metabolism Multiprotein Complexes - metabolism Multiprotein Complexes - chemistry RNA - chemistry DNA - chemistry Hu, Gang oth Yang, Jianyi oth Peng, Zhenling oth Uversky, Vladimir N oth Kurgan, Lukasz oth Enthalten in FEBS letters Amsterdam [u.a.] : Elsevier, 1968 589(2015), 19PartA, Seite 2561-2569 (DE-627)129522023 (DE-600)212746-5 (DE-576)014938014 0014-5793 nnns volume:589 year:2015 number:19PartA pages:2561-2569 http://dx.doi.org/10.1016/j.febslet.2015.08.014 Volltext http://onlinelibrary.wiley.com/doi/10.1016/j.febslet.2015.08.014/abstract http://www.ncbi.nlm.nih.gov/pubmed/26297830 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_21 GBV_ILN_70 GBV_ILN_211 GBV_ILN_2219 GBV_ILN_4012 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4305 AR 589 2015 19PartA 2561-2569 |
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10.1016/j.febslet.2015.08.014 doi PQ20160617 (DE-627)OLC196554777X (DE-599)GBVOLC196554777X (PRQ)c2239-eb44a43fd072197cb5e5f4eb05b59d838e3e966129421358cdb755d870307e610 (KEY)0045922420150000589001902561invariousproteincomplexesdisorderedprotomershavela DE-627 ger DE-627 rakwb eng 570 530 610 DNB Wu, Zhonghua verfasserin aut In various protein complexes, disordered protomers have large per‐residue surface areas and area of protein‐, DNA‐ and RNA‐binding interfaces 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier We provide first large scale analysis of the peculiarities of surface areas of 5658 dissimilar (below 50% sequence similarity) proteins with known 3D‐structures that bind to proteins, DNA or RNAs. We show here that area of the protein surface is highly correlated with the protein length. The size of the interface surface is only modestly correlated with the protein size, except for RNA‐binding proteins where larger proteins are characterized by larger interfaces. Disordered proteins with disordered interfaces are characterized by significantly larger per‐residue areas of their surfaces and interfaces when compared to the structured proteins. These result are applicable for proteins involved in interaction with DNA, RNA, and proteins and suggest that disordered proteins and binding regions are less compact and more likely to assume extended shape. We demonstrate that disordered protein binding residues in the interfaces of disordered proteins drive the increase in the per residue area of these interfaces. Our results can be used to predict in silico whether a given protomer from the DNA, RNA or protein complex is likely to be disordered in its unbound form. Nutzungsrecht: FEBS Letters 589 (2015) 1873-3468 © 2015 Federation of European Biochemical Societies Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. Protein–protein interaction Protein–DNA interaction Protein–RNA interaction Binding interface Intrinsic disorder Binding surface Intrinsically Disordered Proteins - metabolism RNA - metabolism Computational Biology - methods Intrinsically Disordered Proteins - chemistry DNA - metabolism Multiprotein Complexes - metabolism Multiprotein Complexes - chemistry RNA - chemistry DNA - chemistry Hu, Gang oth Yang, Jianyi oth Peng, Zhenling oth Uversky, Vladimir N oth Kurgan, Lukasz oth Enthalten in FEBS letters Amsterdam [u.a.] : Elsevier, 1968 589(2015), 19PartA, Seite 2561-2569 (DE-627)129522023 (DE-600)212746-5 (DE-576)014938014 0014-5793 nnns volume:589 year:2015 number:19PartA pages:2561-2569 http://dx.doi.org/10.1016/j.febslet.2015.08.014 Volltext http://onlinelibrary.wiley.com/doi/10.1016/j.febslet.2015.08.014/abstract http://www.ncbi.nlm.nih.gov/pubmed/26297830 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_21 GBV_ILN_70 GBV_ILN_211 GBV_ILN_2219 GBV_ILN_4012 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4305 AR 589 2015 19PartA 2561-2569 |
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In various protein complexes, disordered protomers have large per‐residue surface areas and area of protein‐, DNA‐ and RNA‐binding interfaces |
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in various protein complexes, disordered protomers have large per‐residue surface areas and area of protein‐, dna‐ and rna‐binding interfaces |
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In various protein complexes, disordered protomers have large per‐residue surface areas and area of protein‐, DNA‐ and RNA‐binding interfaces |
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We provide first large scale analysis of the peculiarities of surface areas of 5658 dissimilar (below 50% sequence similarity) proteins with known 3D‐structures that bind to proteins, DNA or RNAs. We show here that area of the protein surface is highly correlated with the protein length. The size of the interface surface is only modestly correlated with the protein size, except for RNA‐binding proteins where larger proteins are characterized by larger interfaces. Disordered proteins with disordered interfaces are characterized by significantly larger per‐residue areas of their surfaces and interfaces when compared to the structured proteins. These result are applicable for proteins involved in interaction with DNA, RNA, and proteins and suggest that disordered proteins and binding regions are less compact and more likely to assume extended shape. We demonstrate that disordered protein binding residues in the interfaces of disordered proteins drive the increase in the per residue area of these interfaces. Our results can be used to predict in silico whether a given protomer from the DNA, RNA or protein complex is likely to be disordered in its unbound form. |
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We provide first large scale analysis of the peculiarities of surface areas of 5658 dissimilar (below 50% sequence similarity) proteins with known 3D‐structures that bind to proteins, DNA or RNAs. We show here that area of the protein surface is highly correlated with the protein length. The size of the interface surface is only modestly correlated with the protein size, except for RNA‐binding proteins where larger proteins are characterized by larger interfaces. Disordered proteins with disordered interfaces are characterized by significantly larger per‐residue areas of their surfaces and interfaces when compared to the structured proteins. These result are applicable for proteins involved in interaction with DNA, RNA, and proteins and suggest that disordered proteins and binding regions are less compact and more likely to assume extended shape. We demonstrate that disordered protein binding residues in the interfaces of disordered proteins drive the increase in the per residue area of these interfaces. Our results can be used to predict in silico whether a given protomer from the DNA, RNA or protein complex is likely to be disordered in its unbound form. |
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We provide first large scale analysis of the peculiarities of surface areas of 5658 dissimilar (below 50% sequence similarity) proteins with known 3D‐structures that bind to proteins, DNA or RNAs. We show here that area of the protein surface is highly correlated with the protein length. The size of the interface surface is only modestly correlated with the protein size, except for RNA‐binding proteins where larger proteins are characterized by larger interfaces. Disordered proteins with disordered interfaces are characterized by significantly larger per‐residue areas of their surfaces and interfaces when compared to the structured proteins. These result are applicable for proteins involved in interaction with DNA, RNA, and proteins and suggest that disordered proteins and binding regions are less compact and more likely to assume extended shape. We demonstrate that disordered protein binding residues in the interfaces of disordered proteins drive the increase in the per residue area of these interfaces. Our results can be used to predict in silico whether a given protomer from the DNA, RNA or protein complex is likely to be disordered in its unbound form. |
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In various protein complexes, disordered protomers have large per‐residue surface areas and area of protein‐, DNA‐ and RNA‐binding interfaces |
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http://dx.doi.org/10.1016/j.febslet.2015.08.014 http://onlinelibrary.wiley.com/doi/10.1016/j.febslet.2015.08.014/abstract http://www.ncbi.nlm.nih.gov/pubmed/26297830 |
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Hu, Gang Yang, Jianyi Peng, Zhenling Uversky, Vladimir N Kurgan, Lukasz |
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