caa a22 4500 445325941 CHVBK 20180317142720.0 cr unu---uuuuu 170323e20110601xx s 000 0 eng 10.1007/s10858-011-9505-5 doi (NATIONALLICENCE)springer-10.1007/s10858-011-9505-5 Solution structure, dynamics and thermodynamics of the three SH3 domains of CD2AP [Elektronische Daten] [Jose Roldan, Martin Blackledge, Nico van Nuland, Ana Azuaga] 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. Springer Science+Business Media B.V., 2011 Adaptor protein nationallicence CD2AP nationallicence NMR nationallicence Protein structure nationallicence SH3 domain nationallicence CD2AP : CD2 associated protein nationallicence DLS : Dynamic light scattering nationallicence NMR : Nuclear magnetic resonance nationallicence NOESY : Nuclear overhauser enhancement spectroscopy nationallicence RDC : Residual dipolar coupling nationallicence RMSD : Root mean square deviation nationallicence SH3 : Src-homology domain 3 nationallicence DSC : Differential scanning calorimetry nationallicence TOCSY : Total correlation spectroscopy nationallicence Roldan Jose Departamento de Química Física e Instituto de Biotecnología, Facultad de Ciencias, Universidad de Granada, Fuentenueva s/n, 18071, Granada, Spain aut Blackledge Martin Protein Dynamics and Flexibility by NMR, Institut de Biologie Structurale Jean-Pierre Ebel, CEA, CNRS, UJF UMR 5075, 41 Rue Jules Horowitz, 38027, Grenoble, France aut van Nuland Nico Structural Biology Brussels, Vrije Universiteit Brussel, Pleinlaan 2, 1050, Brussels, Belgium aut Azuaga Ana Departamento de Química Física e Instituto de Biotecnología, Facultad de Ciencias, Universidad de Granada, Fuentenueva s/n, 18071, Granada, Spain aut Journal of Biomolecular NMR Springer Netherlands 50/2(2011-06-01), 103-117 0925-2738 50:2<103 2011 50 10858 https://doi.org/10.1007/s10858-011-9505-5 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s10858-011-9505-5 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Roldan Jose Departamento de Química Física e Instituto de Biotecnología, Facultad de Ciencias, Universidad de Granada, Fuentenueva s/n, 18071, Granada, Spain aut NATIONALLICENCE 700 1- Blackledge Martin Protein Dynamics and Flexibility by NMR, Institut de Biologie Structurale Jean-Pierre Ebel, CEA, CNRS, UJF UMR 5075, 41 Rue Jules Horowitz, 38027, Grenoble, France aut NATIONALLICENCE 700 1- van Nuland Nico Structural Biology Brussels, Vrije Universiteit Brussel, Pleinlaan 2, 1050, Brussels, Belgium aut NATIONALLICENCE 700 1- Azuaga Ana Departamento de Química Física e Instituto de Biotecnología, Facultad de Ciencias, Universidad de Granada, Fuentenueva s/n, 18071, Granada, Spain aut NATIONALLICENCE 773 0- Journal of Biomolecular NMR Springer Netherlands 50/2(2011-06-01), 103-117 0925-2738 50:2<103 2011 50 10858 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer