| Autor: |
Feng, S, Kasahara, C, Rickles, R J, Schreiber, S L |
| Zdroj: |
Proceedings of the National Academy of Sciences of the United States of America; December 1995, Vol. 92 Issue: 26 p12408-12415, 8p |
| Abstrakt: |
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. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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