1sha
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(New page: 200px<br /><applet load="1sha" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sha, resolution 1.5Å" /> '''CRYSTAL STRUCTURE OF ...)
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Revision as of 00:15, 21 November 2007
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CRYSTAL STRUCTURE OF THE PHOSPHOTYROSINE RECOGNITION DOMAIN SH2 OF V-SRC COMPLEXED WITH TYROSINE-PHOSPHORYLATED PEPTIDES
Overview
Three-dimensional structures of complexes of the SH2 domain of the v-src, oncogene product with two phosphotyrosyl peptides have been determined by, X-ray crystallography at resolutions of 1.5 and 2.0 A, respectively. A, central antiparallel beta-sheet in the structure is flanked by two, alpha-helices, with peptide binding mediated by the sheet, intervening, loops and one of the helices. The specific recognition of phosphotyrosine, involves amino-aromatic interactions between lysine and arginine side, chains and the ring system in addition to hydrogen-bonding interactions, with the phosphate.
About this Structure
1SHA is a Single protein structure of sequence from Rous sarcoma virus. Active as Transferase, with EC number and 2.7.10.2 2.7.10.1 and 2.7.10.2 Full crystallographic information is available from OCA.
Reference
Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides., Waksman G, Kominos D, Robertson SC, Pant N, Baltimore D, Birge RB, Cowburn D, Hanafusa H, Mayer BJ, Overduin M, et al., Nature. 1992 Aug 20;358(6388):646-53. PMID:1379696
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