Publication Type

Journal Article

Version

publishedVersion

Publication Date

12-2012

Abstract

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.

Keywords

algorithm, beta chain, binding site, catalysis, protein analysis, protein binding, protein database

Discipline

Computer Sciences | Databases and Information Systems

Research Areas

Data Science and Engineering

Publication

PLoS ONE

Volume

7

Issue

12

First Page

e50821-1

Last Page

13

ISSN

1932-6203

Identifier

10.1371/journal.pone.0050821

Publisher

Public Library of Science

Copyright Owner and License

Authors

Creative Commons License

Creative Commons Attribution 4.0 International License
This work is licensed under a Creative Commons Attribution 4.0 International License.

Additional URL

https://doi.org/10.1371/journal.pone.0050821

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