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Interfacial water molecules in SH3 interactions: Getting the full picture on polyproline recognition by protein–protein interaction domains
Author(s) -
Zafra-Ruano Ana,
Luque Irene
Publication year - 2012
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2012.04.057
Subject(s) - polyproline helix , sh3 domain , stacking , molecular recognition , protein–protein interaction , chemistry , molecule , computational biology , proline , biophysics , biology , biochemistry , peptide , signal transduction , amino acid , organic chemistry , proto oncogene tyrosine protein kinase src
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.