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Proc Natl Acad Sci U S A. 1995 Dec 19;92(26):12408-15.

Specific interactions outside the proline-rich core of two classes of Src homology 3 ligands.

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Howard Hughes Medical Institute, Department of Chemistry, Harvard University, Cambridge, MA 02138, USA.


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.

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