2jte Citations

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


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, 1Halpha, 13Calpha, 13CO and 13Cbeta 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.

Reviews citing this publication (1)

  1. Characterizing weak protein-protein complexes by NMR residual dipolar couplings. Jensen MR, Ortega-Roldan JL, Salmon L, van Nuland N, Blackledge M. Eur. Biophys. J. 40 1371-1381 (2011)

Articles citing this publication (8)

  1. Accurate characterization of weak macromolecular interactions by titration of NMR residual dipolar couplings: application to the CD2AP SH3-C:ubiquitin complex. Ortega-Roldan JL, Jensen MR, Brutscher B, Azuaga AI, Blackledge M, van Nuland NA. Nucleic Acids Res. 37 e70 (2009)
  2. Multi-timescale conformational dynamics of the SH3 domain of CD2-associated protein using NMR spectroscopy and accelerated molecular dynamics. Salmon L, Pierce L, Grimm A, Ortega Roldan JL, Mollica L, Jensen MR, van Nuland N, Markwick PR, McCammon JA, Blackledge M. Angew. Chem. Int. Ed. Engl. 51 6103-6106 (2012)
  3. Structure, dynamics, and kinetics of weak protein-protein complexes from NMR spin relaxation measurements of titrated solutions. Salmon L, Ortega Roldan JL, Lescop E, Licinio A, van Nuland N, Jensen MR, Blackledge M. Angew. Chem. Int. Ed. Engl. 50 3755-3759 (2011)
  4. Solution structure, dynamics and thermodynamics of the three SH3 domains of CD2AP. Roldan JL, Blackledge M, van Nuland NA, Azuaga AI. J. Biomol. NMR 50 103-117 (2011)
  5. Multimeric and differential binding of CIN85/CD2AP with two atypical proline-rich sequences from CD2 and Cbl-b*. Ceregido MA, Garcia-Pino A, Ortega-Roldan JL, Casares S, López Mayorga O, Bravo J, van Nuland NA, Azuaga AI. FEBS J. 280 3399-3415 (2013)
  6. Structure of the kidney slit diaphragm adapter protein CD2-associated protein as determined with electron microscopy. Adair BD, Altintas MM, Möller CC, Arnaout MA, Reiser J. J. Am. Soc. Nephrol. 25 1465-1473 (2014)
  7. Differential Recognition Preferences of the Three Src Homology 3 (SH3) Domains from the Adaptor CD2-associated Protein (CD2AP) and Direct Association with Ras and Rab Interactor 3 (RIN3). Rouka E, Simister PC, Janning M, Kumbrink J, Konstantinou T, Muniz JR, Joshi D, O'Reilly N, Volkmer R, Ritter B, Knapp S, von Delft F, Kirsch KH, Feller SM. J. Biol. Chem. 290 25275-25292 (2015)
  8. [Study of the structure and dynamics of a chimeric variant of the SH3 domain (SHA-Bergerac) by NMR spectroscopy] Prokhorov DA, Timchenko MA, Kudrevatykh IuA, Fediukina DV, Gushchina LV, Khristoforov VS, Filimonov VV, Kutyshenko VP. Bioorg. Khim. 34 645-653 (2008)