期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 107, 期 5, 页码 1995-2000出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0908044107
关键词
functional residues; protein family evolution; protein function; protein-protein interfaces; specificity determining positions
资金
- Computational Systems Biology Group (CNB-CSIC)
- CONSOLIDER [CSD2007-00050]
- Spanish Ministry for Education and Science [BIO2007-66855, BIO2006-15318, PIE 200620I240]
- EU [LSHG-CT-2004-503567]
- Spanish National Institute for Bioinformatics (INB)
The divergence accumulated during the evolution of protein families translates into their internal organization as subfamilies, and it is directly reflected in the characteristic patterns of differentially conserved residues. These specifically conserved positions in protein subfamilies are known as specificity determining positions (SDPs). Previous studies have limited their analysis to the study of the relationship between these positions and ligand-binding specificity, demonstrating significant yet limited predictive capacity. We have systematically extended this observation to include the role of differential protein interactions in the segregation of protein subfamilies and explored in detail the structural distribution of SDPs at protein interfaces. Our results show the extensive influence of protein interactions in the evolution of protein families and the widespread association of SDPs with protein interfaces. The combined analysis of SDPs in interfaces and ligand-binding sites provides a more complete picture of the organization of protein families, constituting the necessary framework for a large scale analysis of the evolution of protein function.
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