High-resolution protein–protein docking

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

1 Scopus citations


Advances in the field of protein–protein docking allow us today to create models of protein complexes that approach in quality experimentally derived structures. Crucial to this is the explicit modelling of the conformational changes that the individual protein monomers undergo upon binding. A stringent energy function that allows the distinction between well-packed interfaces and wrong alternatives can then be used to select the correct model. The models can provide important insights into the biological function of the protein–protein interaction, and provide guidance to experimentalists. Thanks to their high resolution, these models are amenable to computational interface design methods that were until recently restricted to experimentally derived structures, thereby opening up the way towards docking-based redesign of interactions, or targeted inhibition. Nevertheless, proteins that undergo larger conformational changes upon binding are still difficult to model, but steady advances in this field allow for optimistic outlooks, even if challenges remain ahead.

Original languageAmerican English
Title of host publicationProtein-Protein Complexes
Subtitle of host publicationAnalysis, Modeling and Drug Design
PublisherImperial College Press
Number of pages27
ISBN (Electronic)9781848163409
ISBN (Print)9781848163386
StatePublished - 1 Jan 2010

Bibliographical note

Publisher Copyright:
© 2010 by Imperial College Press. All rights reserved.


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