Structural and Functional Analysis of Multi-Interface Domains

A multi-interface domain is a domain that can shape multiple and distinctive binding sites to contact with many other domains, forming a hub in domain-domain interaction networks. The functions played by the multiple interfaces are usually different, but there is no strict bijection between the func...

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Vydáno v:PloS one Ročník 7; číslo 12; s. e50821
Hlavní autoři: Zhao, Liang, Hoi, Steven C. H., Wong, Limsoon, Hamp, Tobias, Li, Jinyan
Médium: Journal Article
Jazyk:angličtina
Vydáno: United States Public Library of Science 14.12.2012
Public Library of Science (PLoS)
Témata:
Algorithms
Amino acids
Animals
Binding Sites
Biology
Cluster Analysis
Computer engineering
Crystallography, X-Ray - methods
Data mining
Databases, Protein
Fingerprints
Functional analysis
Graph theory
Humans
Interfaces
International conferences
Ligands
Models, Molecular
Models, Statistical
Molecular Conformation
Packaging
Physics
Proteasome Endopeptidase Complex - chemistry
Protein Binding
Protein Conformation
Protein engineering
Protein Interaction Mapping
Protein Structure, Secondary
Protein Structure, Tertiary
Proteins
Proteins - chemistry
Structure-function relationships
Singapore
ISSN:1932-6203, 1932-6203
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Popis
Shrnutí:A multi-interface domain is a domain that can shape multiple and distinctive binding sites to contact with many other domains, forming a hub in domain-domain interaction networks. The functions played by the multiple interfaces are usually different, but there is no strict bijection between the functions and interfaces as some subsets of the interfaces play the same function. This work applies graph theory and algorithms to discover fingerprints for the multiple interfaces of a domain and to establish associations between the interfaces and functions, based on a huge set of multi-interface proteins from PDB. We found that about 40% of proteins have the multi-interface property, however the involved multi-interface domains account for only a tiny fraction (1.8%) of the total number of domains. The interfaces of these domains are distinguishable in terms of their fingerprints, indicating the functional specificity of the multiple interfaces in a domain. Furthermore, we observed that both cooperative and distinctive structural patterns, which will be useful for protein engineering, exist in the multiple interfaces of a domain.
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Competing Interests: The authors have declared that no competing interests exist.
Conceived and designed the experiments: LZ JL. Performed the experiments: LZ. Analyzed the data: LZ TH. Wrote the paper: LZ SH LW TH JL.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0050821