2JTE
Third SH3 domain of CD2AP
Summary for 2JTE
| Entry DOI | 10.2210/pdb2jte/pdb |
| NMR Information | BMRB: 15407 |
| Descriptor | CD2-associated protein (1 entity in total) |
| Functional Keywords | protein, sh3 domain, coiled coil, cytoplasm, phosphorylation, sh3-binding, signaling protein |
| Biological source | Mus musculus (house mouse) |
| Cellular location | Cytoplasm, cytoskeleton: Q9JLQ0 |
| Total number of polymer chains | 1 |
| Total formula weight | 7146.91 |
| Authors | van Nuland, N.A.J.,Ortega, R.J.,Romero Romero, M.,Ab, E.,Ora, A.,Lopez, M.O.,Azuaga, A.I. (deposition date: 2007-07-28, release date: 2007-12-11, Last modification date: 2024-05-29) |
| Primary citation | Ortega Roldan, J.L.,Romero Romero, M.L.,Ora, A.,Ab, E.,Lopez Mayorga, O.,Azuaga, A.I.,van Nuland, N.A. The high resolution NMR structure of the third SH3 domain of CD2AP. J.Biomol.Nmr, 39:331-336, 2007 Cited by PubMed Abstract: 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. PubMed: 17922258DOI: 10.1007/s10858-007-9201-7 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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