Solution structure,dynamics and thermodynamics of the three SH3 domains of CD2AP |
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| Authors: | Jose L Ortega Roldan Martin Blackledge Nico A J van Nuland Ana I Azuaga |
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| Institution: | 1.Departamento de Química Física e Instituto de Biotecnología, Facultad de Ciencias,Universidad de Granada,Granada,Spain;2.Protein Dynamics and Flexibility by NMR,Institut de Biologie Structurale Jean-Pierre Ebel, CEA, CNRS, UJF UMR 5075,Grenoble,France;3.Structural Biology Brussels,Vrije Universiteit Brussel,Brussels,Belgium;4.Department of Molecular and Cellular Interactions,VIB,Brussels,Belgium |
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| Abstract: | CD2 associated protein (CD2AP) is an adaptor protein that plays an important role in cell to cell union needed for the kidney
function. It contains three N-terminal SH3 domains that are able to interact among others with CD2, ALIX, c-Cbl and Ubiquitin.
To understand the role of the individual SH3 domains of this adaptor protein we have performed a complete structural, thermodynamic
and dynamic characterization of the separate domains using NMR and DSC. The energetic contributions to the stability and the
backbone dynamics have been related to the structural features of each domain using the structure-based FoldX algorithm. We
have found that the N-terminal SH3 domain of both adaptor proteins CD2AP and CIN85 are the most stable SH3 domains that have
been studied until now. This high stability is driven by a more extensive network of intra-molecular interactions. We believe
that this increased stabilization of N-terminal SH3 domains in adaptor proteins is crucial to maintain the necessary conformation
to establish the proper interactions critical for the recruitment of their natural targets. |
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