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

FEBS Letters
Ana Zafra-Ruano, Irene Luque

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.

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Citations

Nov 14, 2013·PloS One·Amanda P WoonAnna Roujeinikova
Jan 12, 2013·Current Protein & Peptide Science·Rita Berisio, Luigi Vitagliano
Sep 30, 2014·The European Journal of Neuroscience·Beatriz G ArmendárizFerran Burgaya
Oct 1, 2013·Computational Biology and Chemistry·Mostafa H AhmedGlen E Kellogg
May 18, 2016·Journal of Computational Chemistry·Maria M Reif, Martin Zacharias
Jun 23, 2016·Biophysical Journal·Veer S BhattJae-Hyun Cho
Mar 10, 2017·Expert Opinion on Drug Discovery·Rafael Claveria-GimenoAdrian Velazquez-Campoy
Oct 23, 2019·Scientific Reports·Manuel Iglesias-BexigaIrene Luque
Jun 10, 2021·Chemical Reviews·Andreas FrutigerNako Nakatsuka
May 6, 2017·Journal of Medicinal Chemistry·Francesca SpyrakisGlen E Kellogg

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