Published August 20, 1992
| public
Journal Article
Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides
Chicago
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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.
Additional Information
© 1992 Nature Publishing Group. Received 21 July 1992; Accepted 05 August 1992; Issue Date 20 August 1992. We thank S. K. Burley, P. Model, X.-P. Kong, G. A. Petsko and T. P. Sakmar for suggestions. S. Nair for references to phenyl phosphate crystal structures, and B. Chait for the mass spectroscopy done at the National Resource for Mass Spectrometric Analysis of Biological Macromolecules. Supported in part by grants and fellowships from the NIH (D.B., D.C., H.H., J.K., B.J.M., C.B.R., M.D.R.), A.C.S. (M.D.R.) and Pew Foundation (J.K., M.D.R.).Additional details
- Eprint ID
- 103191
- Resolver ID
- CaltechAUTHORS:20200513-153340587
- NIH
- American Cancer Society
- Pew Charitable Trust
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