1SHA

CRYSTAL STRUCTURE OF THE PHOSPHOTYROSINE RECOGNITION DOMAIN SH2 OF V-SRC COMPLEXED WITH TYROSINE-PHOSPHORYLATED PEPTIDES

Summary for 1SHA

Entry DOI	10.2210/pdb1sha/pdb
Descriptor	V-SRC SH2 DOMAIN, PHOSPHOPEPTIDE A (3 entities in total)
Functional Keywords	phosphotransferase
Biological source	Rous sarcoma virus More
Total number of polymer chains	2
Total formula weight	12672.25
Authors	Waksman, G.,Kuriyan, J. (deposition date: 1992-08-18, release date: 1993-10-31, Last modification date: 2024-10-30)
Primary citation	Waksman, G.,Kominos, D.,Robertson, S.C.,Pant, N.,Baltimore, D.,Birge, R.B.,Cowburn, D.,Hanafusa, H.,Mayer, B.J.,Overduin, M.,Resh, M.D.,Rios, C.B.,Silverman, L.,Kuriyan, J. Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides. Nature, 358:646-653, 1992 Cited by PubMed Abstract: 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. PubMed: 1379696 DOI: 10.1038/358646a0 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.5 Å)

Structure validation