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

Hongtao Yu, Michael K. Rosen, Tae Bum Shin, Cynthia Seidel-Dugan, Joan S. Brugge, Stuart L. Schreiber

Research output: Contribution to journalArticle

274 Scopus citations

Abstract

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 β 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.

Original languageEnglish (US)
Pages (from-to)1665-1668
Number of pages4
JournalScience
Volume258
Issue number5088
DOIs
StatePublished - Jan 1 1992

ASJC Scopus subject areas

  • General

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    Yu, H., Rosen, M. K., Shin, T. B., Seidel-Dugan, C., Brugge, J. S., & Schreiber, S. L. (1992). Solution structure of the SH3 domain of Src and identification of its ligand-binding site. Science, 258(5088), 1665-1668. https://doi.org/10.1126/science.1280858