PDZ DOMAINS AND THE ORGANIZATION OF SUPRAMOLECULAR COMPLEXES
Abstract PDZ domains are modular protein interaction domains that bind in a sequence-specific fashion to short C-terminal peptides or internal peptides that fold in a beta-finger. The diversity of PDZ binding specificities can be explained by variable amino acids lining the peptide-binding groove of...
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E-Artikel |
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| Erschienen: |
2001 |
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29 |
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| Reproduktion: |
Annual Reviews Electronic Back Volume Collection 1932-2005ff |
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| Übergeordnetes Werk: |
in: Annual review of neuroscience - Palo Alto, Calif. : Annual Review Inc., 1978, 24(2001), Seite 1-29 |
| Übergeordnetes Werk: |
volume:24 ; year:2001 ; pages:1-29 ; extent:29 |
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| 520 | |a Abstract PDZ domains are modular protein interaction domains that bind in a sequence-specific fashion to short C-terminal peptides or internal peptides that fold in a beta-finger. The diversity of PDZ binding specificities can be explained by variable amino acids lining the peptide-binding groove of the PDZ domain. Abundantly represented in Caenorhabditis elegans, Drosophila melanogaster, and mammalian genomes, PDZ domains are frequently found in multiple copies or are associated with other protein-binding motifs in multidomain scaffold proteins. PDZ-containing proteins are typically involved in the assembly of supramolecular complexes that perform localized signaling functions at particular subcellular locations. Organization around a PDZ-based scaffold allows the stable localization of interacting proteins and enhances the rate and fidelity of signal transduction within the complex. Some PDZ-containing proteins are more dynamically regulated in distribution and may also be involved in the trafficking of interacting proteins within the cell. | ||
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(DE-627)NLEJ164154299 DE-627 ger DE-627 rakwb PDZ DOMAINS AND THE ORGANIZATION OF SUPRAMOLECULAR COMPLEXES 2001 29 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract PDZ domains are modular protein interaction domains that bind in a sequence-specific fashion to short C-terminal peptides or internal peptides that fold in a beta-finger. The diversity of PDZ binding specificities can be explained by variable amino acids lining the peptide-binding groove of the PDZ domain. Abundantly represented in Caenorhabditis elegans, Drosophila melanogaster, and mammalian genomes, PDZ domains are frequently found in multiple copies or are associated with other protein-binding motifs in multidomain scaffold proteins. PDZ-containing proteins are typically involved in the assembly of supramolecular complexes that perform localized signaling functions at particular subcellular locations. Organization around a PDZ-based scaffold allows the stable localization of interacting proteins and enhances the rate and fidelity of signal transduction within the complex. Some PDZ-containing proteins are more dynamically regulated in distribution and may also be involved in the trafficking of interacting proteins within the cell. Annual Reviews Electronic Back Volume Collection 1932-2005ff Sheng, Morgan oth Sala, Carlo oth in Annual review of neuroscience Palo Alto, Calif. : Annual Review Inc., 1978 24(2001), Seite 1-29 Online-Ressource (DE-627)NLEJ164018913 (DE-600)1470452-3 nnns volume:24 year:2001 pages:1-29 extent:29 http://dx.doi.org/10.1146/annurev.neuro.24.1.1 text/html Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-ANR GBV_NL_ARTICLE AR 24 2001 1-29 29 |
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(DE-627)NLEJ164154299 DE-627 ger DE-627 rakwb PDZ DOMAINS AND THE ORGANIZATION OF SUPRAMOLECULAR COMPLEXES 2001 29 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract PDZ domains are modular protein interaction domains that bind in a sequence-specific fashion to short C-terminal peptides or internal peptides that fold in a beta-finger. The diversity of PDZ binding specificities can be explained by variable amino acids lining the peptide-binding groove of the PDZ domain. Abundantly represented in Caenorhabditis elegans, Drosophila melanogaster, and mammalian genomes, PDZ domains are frequently found in multiple copies or are associated with other protein-binding motifs in multidomain scaffold proteins. PDZ-containing proteins are typically involved in the assembly of supramolecular complexes that perform localized signaling functions at particular subcellular locations. Organization around a PDZ-based scaffold allows the stable localization of interacting proteins and enhances the rate and fidelity of signal transduction within the complex. Some PDZ-containing proteins are more dynamically regulated in distribution and may also be involved in the trafficking of interacting proteins within the cell. Annual Reviews Electronic Back Volume Collection 1932-2005ff Sheng, Morgan oth Sala, Carlo oth in Annual review of neuroscience Palo Alto, Calif. : Annual Review Inc., 1978 24(2001), Seite 1-29 Online-Ressource (DE-627)NLEJ164018913 (DE-600)1470452-3 nnns volume:24 year:2001 pages:1-29 extent:29 http://dx.doi.org/10.1146/annurev.neuro.24.1.1 text/html Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-ANR GBV_NL_ARTICLE AR 24 2001 1-29 29 |
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(DE-627)NLEJ164154299 DE-627 ger DE-627 rakwb PDZ DOMAINS AND THE ORGANIZATION OF SUPRAMOLECULAR COMPLEXES 2001 29 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract PDZ domains are modular protein interaction domains that bind in a sequence-specific fashion to short C-terminal peptides or internal peptides that fold in a beta-finger. The diversity of PDZ binding specificities can be explained by variable amino acids lining the peptide-binding groove of the PDZ domain. Abundantly represented in Caenorhabditis elegans, Drosophila melanogaster, and mammalian genomes, PDZ domains are frequently found in multiple copies or are associated with other protein-binding motifs in multidomain scaffold proteins. PDZ-containing proteins are typically involved in the assembly of supramolecular complexes that perform localized signaling functions at particular subcellular locations. Organization around a PDZ-based scaffold allows the stable localization of interacting proteins and enhances the rate and fidelity of signal transduction within the complex. Some PDZ-containing proteins are more dynamically regulated in distribution and may also be involved in the trafficking of interacting proteins within the cell. Annual Reviews Electronic Back Volume Collection 1932-2005ff Sheng, Morgan oth Sala, Carlo oth in Annual review of neuroscience Palo Alto, Calif. : Annual Review Inc., 1978 24(2001), Seite 1-29 Online-Ressource (DE-627)NLEJ164018913 (DE-600)1470452-3 nnns volume:24 year:2001 pages:1-29 extent:29 http://dx.doi.org/10.1146/annurev.neuro.24.1.1 text/html Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-ANR GBV_NL_ARTICLE AR 24 2001 1-29 29 |
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(DE-627)NLEJ164154299 DE-627 ger DE-627 rakwb PDZ DOMAINS AND THE ORGANIZATION OF SUPRAMOLECULAR COMPLEXES 2001 29 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract PDZ domains are modular protein interaction domains that bind in a sequence-specific fashion to short C-terminal peptides or internal peptides that fold in a beta-finger. The diversity of PDZ binding specificities can be explained by variable amino acids lining the peptide-binding groove of the PDZ domain. Abundantly represented in Caenorhabditis elegans, Drosophila melanogaster, and mammalian genomes, PDZ domains are frequently found in multiple copies or are associated with other protein-binding motifs in multidomain scaffold proteins. PDZ-containing proteins are typically involved in the assembly of supramolecular complexes that perform localized signaling functions at particular subcellular locations. Organization around a PDZ-based scaffold allows the stable localization of interacting proteins and enhances the rate and fidelity of signal transduction within the complex. Some PDZ-containing proteins are more dynamically regulated in distribution and may also be involved in the trafficking of interacting proteins within the cell. Annual Reviews Electronic Back Volume Collection 1932-2005ff Sheng, Morgan oth Sala, Carlo oth in Annual review of neuroscience Palo Alto, Calif. : Annual Review Inc., 1978 24(2001), Seite 1-29 Online-Ressource (DE-627)NLEJ164018913 (DE-600)1470452-3 nnns volume:24 year:2001 pages:1-29 extent:29 http://dx.doi.org/10.1146/annurev.neuro.24.1.1 text/html Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-ANR GBV_NL_ARTICLE AR 24 2001 1-29 29 |
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(DE-627)NLEJ164154299 DE-627 ger DE-627 rakwb PDZ DOMAINS AND THE ORGANIZATION OF SUPRAMOLECULAR COMPLEXES 2001 29 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract PDZ domains are modular protein interaction domains that bind in a sequence-specific fashion to short C-terminal peptides or internal peptides that fold in a beta-finger. The diversity of PDZ binding specificities can be explained by variable amino acids lining the peptide-binding groove of the PDZ domain. Abundantly represented in Caenorhabditis elegans, Drosophila melanogaster, and mammalian genomes, PDZ domains are frequently found in multiple copies or are associated with other protein-binding motifs in multidomain scaffold proteins. PDZ-containing proteins are typically involved in the assembly of supramolecular complexes that perform localized signaling functions at particular subcellular locations. Organization around a PDZ-based scaffold allows the stable localization of interacting proteins and enhances the rate and fidelity of signal transduction within the complex. Some PDZ-containing proteins are more dynamically regulated in distribution and may also be involved in the trafficking of interacting proteins within the cell. Annual Reviews Electronic Back Volume Collection 1932-2005ff Sheng, Morgan oth Sala, Carlo oth in Annual review of neuroscience Palo Alto, Calif. : Annual Review Inc., 1978 24(2001), Seite 1-29 Online-Ressource (DE-627)NLEJ164018913 (DE-600)1470452-3 nnns volume:24 year:2001 pages:1-29 extent:29 http://dx.doi.org/10.1146/annurev.neuro.24.1.1 text/html Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-ANR GBV_NL_ARTICLE AR 24 2001 1-29 29 |
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PDZ DOMAINS AND THE ORGANIZATION OF SUPRAMOLECULAR COMPLEXES |
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Abstract PDZ domains are modular protein interaction domains that bind in a sequence-specific fashion to short C-terminal peptides or internal peptides that fold in a beta-finger. The diversity of PDZ binding specificities can be explained by variable amino acids lining the peptide-binding groove of the PDZ domain. Abundantly represented in Caenorhabditis elegans, Drosophila melanogaster, and mammalian genomes, PDZ domains are frequently found in multiple copies or are associated with other protein-binding motifs in multidomain scaffold proteins. PDZ-containing proteins are typically involved in the assembly of supramolecular complexes that perform localized signaling functions at particular subcellular locations. Organization around a PDZ-based scaffold allows the stable localization of interacting proteins and enhances the rate and fidelity of signal transduction within the complex. Some PDZ-containing proteins are more dynamically regulated in distribution and may also be involved in the trafficking of interacting proteins within the cell. |
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Abstract PDZ domains are modular protein interaction domains that bind in a sequence-specific fashion to short C-terminal peptides or internal peptides that fold in a beta-finger. The diversity of PDZ binding specificities can be explained by variable amino acids lining the peptide-binding groove of the PDZ domain. Abundantly represented in Caenorhabditis elegans, Drosophila melanogaster, and mammalian genomes, PDZ domains are frequently found in multiple copies or are associated with other protein-binding motifs in multidomain scaffold proteins. PDZ-containing proteins are typically involved in the assembly of supramolecular complexes that perform localized signaling functions at particular subcellular locations. Organization around a PDZ-based scaffold allows the stable localization of interacting proteins and enhances the rate and fidelity of signal transduction within the complex. Some PDZ-containing proteins are more dynamically regulated in distribution and may also be involved in the trafficking of interacting proteins within the cell. |
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Abstract PDZ domains are modular protein interaction domains that bind in a sequence-specific fashion to short C-terminal peptides or internal peptides that fold in a beta-finger. The diversity of PDZ binding specificities can be explained by variable amino acids lining the peptide-binding groove of the PDZ domain. Abundantly represented in Caenorhabditis elegans, Drosophila melanogaster, and mammalian genomes, PDZ domains are frequently found in multiple copies or are associated with other protein-binding motifs in multidomain scaffold proteins. PDZ-containing proteins are typically involved in the assembly of supramolecular complexes that perform localized signaling functions at particular subcellular locations. Organization around a PDZ-based scaffold allows the stable localization of interacting proteins and enhances the rate and fidelity of signal transduction within the complex. Some PDZ-containing proteins are more dynamically regulated in distribution and may also be involved in the trafficking of interacting proteins within the cell. |
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