Abstract
Two dodecapeptides belonging to distinct classes of Src homology 3 (SH3) ligands and selected from biased phage display libraries were used to investigate interactions between a specificity pocket in the Src SH3 domain and ligant residues flanking the proline-rich core. The solution structures of c-Src SH3 complexed with these peptides were solved by NMR. In addition to proline-rich, polyproline type II helix-forming core, the class I and II ligands each possesses a flanking sequence that occupies a large pocket between the RT and n-Src loops of the SH3 domain. Structural and mutational analyses illustrate how the two classes of SH3 ligands exploit a specificity pocket on the receptor differently to increase binding affinity and specificity.
Dates
Type | When |
---|---|
Created | 19 years, 3 months ago (May 31, 2006, 9:26 a.m.) |
Deposited | 3 years, 4 months ago (April 13, 2022, 2:02 p.m.) |
Indexed | 3 weeks, 6 days ago (Aug. 6, 2025, 9:54 a.m.) |
Issued | 29 years, 8 months ago (Dec. 19, 1995) |
Published | 29 years, 8 months ago (Dec. 19, 1995) |
Published Online | 29 years, 8 months ago (Dec. 19, 1995) |
Published Print | 29 years, 8 months ago (Dec. 19, 1995) |
@article{Feng_1995, title={Specific interactions outside the proline-rich core of two classes of Src homology 3 ligands.}, volume={92}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.92.26.12408}, DOI={10.1073/pnas.92.26.12408}, number={26}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Feng, S and Kasahara, C and Rickles, R J and Schreiber, S L}, year={1995}, month=dec, pages={12408–12415} }