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The PAM domain, a multi-protein complex-associated module with an all-alpha-helix fold
BACKGROUND: Multimeric protein complexes have a role in many cellular pathways and are highly interconnected with various other proteins. The characterization of their domain composition and organization provides useful information on the specific role of each region of their sequence. RESULTS: We i...
Autores principales: | , , |
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Formato: | Texto |
Lenguaje: | English |
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BioMed Central
2003
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC319699/ https://www.ncbi.nlm.nih.gov/pubmed/14687415 http://dx.doi.org/10.1186/1471-2105-4-64 |
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author | Ciccarelli, Francesca D Izaurralde, Elisa Bork, Peer |
author_facet | Ciccarelli, Francesca D Izaurralde, Elisa Bork, Peer |
author_sort | Ciccarelli, Francesca D |
collection | PubMed |
description | BACKGROUND: Multimeric protein complexes have a role in many cellular pathways and are highly interconnected with various other proteins. The characterization of their domain composition and organization provides useful information on the specific role of each region of their sequence. RESULTS: We identified a new module, the PAM domain (PCI/PINT associated module), present in single subunits of well characterized multiprotein complexes, like the regulatory lid of the 26S proteasome, the COP-9 signalosome and the Sac3-Thp1 complex. This module is an around 200 residue long domain with a predicted TPR-like all-alpha-helical fold. CONCLUSIONS: The occurrence of the PAM domain in specific subunits of multimeric protein complexes, together with the role of other all-alpha-helical folds in protein-protein interactions, suggest a function for this domain in mediating transient binding to diverse target proteins. |
format | Text |
id | pubmed-319699 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2003 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-3196992004-01-27 The PAM domain, a multi-protein complex-associated module with an all-alpha-helix fold Ciccarelli, Francesca D Izaurralde, Elisa Bork, Peer BMC Bioinformatics Research Article BACKGROUND: Multimeric protein complexes have a role in many cellular pathways and are highly interconnected with various other proteins. The characterization of their domain composition and organization provides useful information on the specific role of each region of their sequence. RESULTS: We identified a new module, the PAM domain (PCI/PINT associated module), present in single subunits of well characterized multiprotein complexes, like the regulatory lid of the 26S proteasome, the COP-9 signalosome and the Sac3-Thp1 complex. This module is an around 200 residue long domain with a predicted TPR-like all-alpha-helical fold. CONCLUSIONS: The occurrence of the PAM domain in specific subunits of multimeric protein complexes, together with the role of other all-alpha-helical folds in protein-protein interactions, suggest a function for this domain in mediating transient binding to diverse target proteins. BioMed Central 2003-12-19 /pmc/articles/PMC319699/ /pubmed/14687415 http://dx.doi.org/10.1186/1471-2105-4-64 Text en Copyright © 2003 Ciccarelli et al; licensee BioMed Central Ltd. This is an Open Access article: verbatim copying and redistribution of this article are permitted in all media for any purpose, provided this notice is preserved along with the article's original URL. |
spellingShingle | Research Article Ciccarelli, Francesca D Izaurralde, Elisa Bork, Peer The PAM domain, a multi-protein complex-associated module with an all-alpha-helix fold |
title | The PAM domain, a multi-protein complex-associated module with an all-alpha-helix fold |
title_full | The PAM domain, a multi-protein complex-associated module with an all-alpha-helix fold |
title_fullStr | The PAM domain, a multi-protein complex-associated module with an all-alpha-helix fold |
title_full_unstemmed | The PAM domain, a multi-protein complex-associated module with an all-alpha-helix fold |
title_short | The PAM domain, a multi-protein complex-associated module with an all-alpha-helix fold |
title_sort | pam domain, a multi-protein complex-associated module with an all-alpha-helix fold |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC319699/ https://www.ncbi.nlm.nih.gov/pubmed/14687415 http://dx.doi.org/10.1186/1471-2105-4-64 |
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