4.3 Review

Prediction and redesign of protein-protein interactions

Journal

PROGRESS IN BIOPHYSICS & MOLECULAR BIOLOGY
Volume 116, Issue 2-3, Pages 194-202

Publisher

PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.pbiomolbio.2014.05.004

Keywords

Evolutionary trace; Protein-protein interaction networks; Functional sites; Molecular evolution; Functional annotation; Protein design

Funding

  1. National Institutes of Health [NIH-GM079656, NIH-GM066099, NLM 5T15LM07093]
  2. National Science Foundation (NSF) [CCF-0905536, DBI-1062455]
  3. Div Of Biological Infrastructure
  4. Direct For Biological Sciences [1062455] Funding Source: National Science Foundation

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Understanding the molecular basis of protein function remains a central goal of biology, with the hope to elucidate the role of human genes in health and in disease, and to rationally design therapies through targeted molecular perturbations. We review here some of the computational techniques and resources available for characterizing a critical aspect of protein function - those mediated by protein-protein interactions (PPI). We describe several applications and recent successes of the Evolutionary Trace (ET) in identifying molecular events and shapes that underlie protein function and specificity in both eukaryotes and prokaryotes. ET is a part of analytical approaches based on the successes and failures of evolution that enable the rational control of PPI. (C) 2014 Elsevier Ltd. All rights reserved.

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