Campus Units

Genetics, Development and Cell Biology, Bioinformatics and Computational Biology

Document Type

Article

Publication Version

Published Version

Publication Date

2015

Journal or Book Title

FEBS Letters

Volume

589

Issue

23

First Page

3516

Last Page

3526

DOI

10.1016/j.febslet.2015.10.003

Abstract

Reliably pinpointing which specific amino acid residues form the interface(s) between a protein and its binding partner(s) is critical for understanding the structural and physicochemical determinants of protein recognition and binding affinity, and has wide applications in modeling and validating protein interactions predicted by high-throughput methods, in engineering proteins, and in prioritizing drug targets. Here, we review the basic concepts, principles and recent advances in computational approaches to the analysis and prediction of protein–protein interfaces. We point out caveats for objectively evaluating interface predictors, and discuss various applications of data-driven interface predictors for improving energy model-driven protein–protein docking. Finally, we stress the importance of exploiting binding partner information in reliably predicting interfaces and highlight recent advances in this emerging direction.

Comments

This article is from FEBS Letters 589 (2015): 3516, doi: 10.1016/j.febslet.2015.10.003. Posted with permission.

Rights

This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).

Copyright Owner

The Authors

Language

en

File Format

application/pdf

Share

COinS