Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides Journal Article


Authors: 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.
Article Title: Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides
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 Å, respectively. A central antiparallel β-sheet in the structure is flanked by two α-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. © 1992 Nature Publishing Group.
Keywords: signal transduction; nonhuman; comparative study; protein conformation; complex formation; protein binding; gene product; protein tyrosine kinase; tyrosine; amino acid sequence; molecular sequence data; sequence alignment; molecular recognition; peptides; crystal structure; models, molecular; binding sites; solvents; phosphotyrosine; crystallography; virus oncogene; x-ray diffraction; protein-tyrosine kinase; oncogene protein pp60(v-src); priority journal; article; support, non-u.s. gov't; support, u.s. gov't, p.h.s.; macromolecular systems
Journal Title: Nature
Volume: 358
Issue: 6388
ISSN: 0028-0836
Publisher: Nature Publishing Group  
Date Published: 1992-08-20
Start Page: 646
End Page: 653
Language: English
DOI: 10.1038/358646a0
PUBMED: 1379696
PROVIDER: scopus
DOI/URL:
Notes: Source: Scopus
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  1. Marilyn D Resh
    120 Resh