Journal of Biomolecular NMR

, Volume 39, Issue 4, pp 331–336 | Cite as

The high resolution NMR structure of the third SH3 domain of CD2AP

  • Jose L. Ortega Roldan
  • M. Luisa Romero Romero
  • Ari Ora
  • Eiso AB
  • Obdulio Lopez Mayorga
  • Ana I. Azuaga
  • Nico A. J. van NulandEmail author
NMR Structure Note


CD2 associated protein (CD2AP) is an adaptor protein that plays an important role in cell to cell union needed for the kidney function. CD2AP interacts, as an adaptor protein, with different natural targets, such as CD2, nefrin, c-Cbl and podocin. These proteins are believed to interact to one of the three SH3 domains that are positioned in the N-terminal region of CD2AP. To understand the network of interactions between the natural targets and the three SH3 domains (SH3-A, B and C), we have started to determine the structures of the individual SH3 domains. Here we present the high-resolution structure of the SH3-C domain derived from NMR data. Full backbone and side-chain assignments were obtained from triple-resonance spectra. The structure was determined from distance restraints derived from high-resolution 600 and 800 MHz NOESY spectra, together with phi and psi torsion angle restraints based on the analysis of 1HN, 15N, 1Hα, 13Cα, 13CO and 13Cβ chemical shifts. Structures were calculated using CYANA and refined in water using RECOORD. The three-dimensional structure of CD2AP SH3-C contains all the features that are typically found in other SH3 domains, including the general binding site for the recognition of polyproline sequences.


Adaptor protein CD2AP NMR Protein structure SH3 domain 



Src-homology domain 3


The third SH3 domain of CD2AP


CD2 associated protein


Nuclear Magnetic Resonance


Nuclear Overhauser enhancement spectroscopy


Total correlation spectroscopy


Root mean square deviation



This research is funded by grant BIO2005-04650 from the Spanish Ministry of Education and Science (MEC), the European Science Foundation EUROCORES Programme and contract ERAS-CT-2003-980409 from the European Union. We thank Adrien Favier for the use of SmartNotebook, Salvador Casares for useful discussions and Pedro L. Mateo for his continuous support. J.L.O.R. and M.LR.R. are supported by a FPU and FPI pre-doctoral grant from the MEC, respectively. A.I.A. is a recipient of a Return research contract from the Junta de Andalucia and N.A.J.v.N. is a recipient of a Ramón y Cajal research contract from the MEC. The 600 MHz spectra were recorded in the Centre for Scientific Instrumentation (CIC) of the University of Granada. The 800 MHz spectra were recorded at the RALF Large Scale Facility in Grenoble, which is funded by the ‘Access to Research Infrastructures’ program of the European Union.


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Copyright information

© Springer Science+Business Media B.V. 2007

Authors and Affiliations

  • Jose L. Ortega Roldan
    • 1
  • M. Luisa Romero Romero
    • 1
  • Ari Ora
    • 2
  • Eiso AB
    • 3
  • Obdulio Lopez Mayorga
    • 1
  • Ana I. Azuaga
    • 1
  • Nico A. J. van Nuland
    • 1
    Email author
  1. 1.Departamento de Química Física e Instituto de Biotecnología, Facultad de CienciasUniversidad de GranadaGranadaSpain
  2. 2.Department of Biosciences/Institute of BiotechnologyUniversity of HelsinkiHelsinkiFinland
  3. 3.Gorlaeus LaboratoryLeiden UniversityLeidenThe Netherlands

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