Interfacial water molecules in SH3 interactions: Getting the full picture on polyproline recognition by protein-protein interaction domains

14Citations
Citations of this article
39Readers
Mendeley users who have this article in their library.

Abstract

The recognition of proline-rich sequences by protein-protein interaction modules is essential for many cellular processes. Nonetheless, in spite of the wealth of structural and functional information collected over the last two decades, polyproline recognition is still not well understood. The patent inconsistency between the generally accepted description of SH3 interactions, based primarily on the stacking of hydrophobic surfaces, and their markedly exothermic character is a clear illustration of the higher complexity of these systems. Here we review the structural and thermodynamic evidence revealing the need for a revision of the current binding paradigm, incomplete and clearly insufficient for a full understanding of binding affinity and specificity, to include interfacial water molecules as universal and relevant elements in polyproline recognition. © 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Cite

CITATION STYLE

APA

Zafra-Ruano, A., & Luque, I. (2012, August 14). Interfacial water molecules in SH3 interactions: Getting the full picture on polyproline recognition by protein-protein interaction domains. FEBS Letters. https://doi.org/10.1016/j.febslet.2012.04.057

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free