2jte
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(New page: 200px<br /><applet load="2jte" size="350" color="white" frame="true" align="right" spinBox="true" caption="2jte" /> '''Third SH3 domain of CD2AP'''<br /> ==Overvi...)
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Revision as of 09:42, 23 January 2008
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Third SH3 domain of CD2AP
Overview
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.
About this Structure
2JTE is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
The high resolution NMR structure of the third SH3 domain of CD2AP., Ortega Roldan JL, Romero Romero ML, Ora A, Ab E, Lopez Mayorga O, Azuaga AI, van Nuland NA, J Biomol NMR. 2007 Dec;39(4):331-6. Epub 2007 Oct 9. PMID:17922258
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