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Bioinformatics Advance Access published online on July 14, 2006
Bioinformatics, doi:10.1093/bioinformatics/btl390
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© 2006 The Author(s)
Received May 24, 2006
Revised July 7, 2006
Accepted July 10, 2006

Article

Global topological features of cancer proteins in the human interactome

Pall F. Jonsson 1 and Paul A. Bates 1 *

1 Biomolecular Modelling Laboratory, Cancer Research UK London Research Institute, 44 Lincoln's Inn Fields, London, WC2A 3PX, UK

* To whom correspondence should be addressed.
Paul A. Bates, E-mail: paul.bates{at}cancer.org.uk


  Abstract

Motivation: The study of interactomes, or networks of protein-protein interactions, is increasingly providing valuable information on biological systems. Here we report a study of cancer proteins in an extensive human protein-protein interaction network constructed by computational methods.

Results: We show that human proteins translated from known cancer genes exhibit a network topology that is different from that of proteins not documented as being mutated in cancer. In particular, cancer proteins show an increase in the number of proteins they interact with. They also appear to participate in central hubs rather than peripheral ones, mirroring their greater centrality and participation in networks that form the backbone of the proteome. Moreover, we show that cancer proteins contain a high ratioof highly promiscuous structural domains, that is, domains with a high propensity for mediating protein interactions. These observations indicate an underlying evolutionary distinction between the two groups of proteins, reflecting the central roles of proteins, whose mutations lead to cancer.

Supplementary information: The interactome data are available though the PIP (Potential Interactions of Proteins) web server at http://bmm.cancerresearchuk.org/servers/pip. Further additional material is available at http://bmm.cancerresearchuk.org/servers/pip/bioinformatics/.

Associate Editor: Jonathan Wren
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