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 |