Solution structure, dynamics and thermodynamics of the three SH3 domains of CD2AP

  • Jose L. Ortega Roldan
  • Martin Blackledge
  • Nico A. J. van Nuland
  • Ana I. Azuaga

DOI: 10.1007/s10858-011-9505-5

Cite this article as:
Roldan, J.L.O., Blackledge, M., van Nuland, N.A.J. et al. J Biomol NMR (2011) 50: 103. doi:10.1007/s10858-011-9505-5


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.


Adaptor protein CD2AP NMR Protein structure SH3 domain 



CD2 associated protein


Dynamic light scattering


Nuclear magnetic resonance


Nuclear overhauser enhancement spectroscopy


Residual dipolar coupling


Root mean square deviation


Src-homology domain 3


Differential scanning calorimetry


Total correlation spectroscopy

Copyright information

© Springer Science+Business Media B.V. 2011

Authors and Affiliations

  • Jose L. Ortega Roldan
    • 1
  • Martin Blackledge
    • 2
  • Nico A. J. van Nuland
    • 3
    • 4
  • Ana I. Azuaga
    • 1
  1. 1.Departamento de Química Física e Instituto de Biotecnología, Facultad de CienciasUniversidad de GranadaGranadaSpain
  2. 2.Protein Dynamics and Flexibility by NMRInstitut de Biologie Structurale Jean-Pierre Ebel, CEA, CNRS, UJF UMR 5075GrenobleFrance
  3. 3.Structural Biology BrusselsVrije Universiteit BrusselBrusselsBelgium
  4. 4.Department of Molecular and Cellular InteractionsVIBBrusselsBelgium

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