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Science 4 December 1992:
Vol. 258. no. 5088, pp. 1665 - 1668
DOI: 10.1126/science.1280858
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Articles

Science, Vol 258, Issue 5088, 1665-1668
Copyright © 1992 by American Association for the Advancement of Science

articles

Solution structure of the SH3 domain of Src and identification of its ligand-binding site

H Yu, MK Rosen, TB Shin, C Seidel-Dugan, JS Brugge, and SL Schreiber

Department of Chemistry, Harvard University, Cambridge, MA 02138.

The Src homology 3 (SH3) region is a protein domain of 55 to 75 amino acids found in many cytoplasmic proteins, including those that participate in signal transduction pathways. The solution structure of the SH3 domain of the tyrosine kinase Src was determined by multidimensional nuclear magnetic resonance methods. The molecule is composed of two short three-stranded anti-parallel beta sheets packed together at approximately right angles. Studies of the SH3 domain bound to proline-rich peptide ligands revealed a hydrophobic binding site on the surface of the protein that is lined with the side chains of conserved aromatic amino acids.


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