| Literature DB >> 1379696 |
G Waksman1, D Kominos, S C Robertson, N Pant, D Baltimore, R B Birge, D Cowburn, H Hanafusa, B J Mayer, M Overduin, M D Resh, C B Rios, L Silverman, J Kuriyan.
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.Entities:
Mesh：
Substances：
Year: 1992 PMID： 1379696 DOI： 10.1038/358646a0
Source DB: PubMed Journal: Nature ISSN： 0028-0836 Impact factor: 49.962