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. Nuland

Research output: Contribution to journalArticleScientificpeer-review

13 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)331-336
Number of pages6
Issue number4
Publication statusPublished - 1 Dec 2007
MoE publication typeA1 Journal article-refereed


  • Adaptor protein
  • CD2AP
  • NMR
  • Protein structure
  • SH3 domain


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