Waksman, Gabriel and Shoelson, S. and Pant, N. and Cowburn, D. and Kuriyan, J. (1993) Binding of a high affinity phosphotyrosyl peptide to the src SH2 domain: crystal structures of the complexed and peptide-free forms. Cell 72 (5), pp. 779-790. ISSN 0092-8674.
Abstract
The crystal structure of the Src SH2 domain complexed with a high affinity 11-residue phosphopeptide has been determined at 2.7 Å resolution by X-ray diffraction. The peptide binds in an extended conformation and makes primary interactions with the SH2 domain at six central residues: PQ(pY)EEI. The phosphotyrosine and the isoleucine are tightly bound by two well-defined pockets on the protein surface, resulting in a complex that resembles a two-pronged plug engaging a two-holed socket. The glutamate residues are in solvent-exposed environments in the vicinity of basic side chains of the SH2 domain, and the two N-terminal residues cap the phosphotyrosine-binding site. The crystal structure of Src SH2 in the absence of peptide has been determined at 2.5 Å resolution, and comparison with the structure of the high affinity complex reveals only localized and relatively small changes.
Metadata
| Item Type: | Article |
|---|---|
| School: | Birkbeck Faculties and Schools > Faculty of Science > School of Natural Sciences |
| Depositing User: | Sarah Hall |
| Date Deposited: | 29 Apr 2019 15:52 |
| Last Modified: | 02 Aug 2023 17:51 |
| URI: | https://eprints.bbk.ac.uk/id/eprint/27352 |
Statistics
Additional statistics are available via IRStats2.
Archive Staff Only (login required)
