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.
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Dates
Type | When |
---|---|
Created | 18 years, 10 months ago (Oct. 5, 2006, 7:03 p.m.) |
Deposited | 1 year, 7 months ago (Jan. 10, 2024, 4:05 p.m.) |
Indexed | 4 weeks ago (July 30, 2025, 11:03 a.m.) |
Issued | 32 years, 8 months ago (Dec. 4, 1992) |
Published | 32 years, 8 months ago (Dec. 4, 1992) |
Published Print | 32 years, 8 months ago (Dec. 4, 1992) |
@article{Yu_1992, title={Solution Structure of the SH3 Domain of Src and Identification of Its Ligand-Binding Site}, volume={258}, ISSN={1095-9203}, url={http://dx.doi.org/10.1126/science.1280858}, DOI={10.1126/science.1280858}, number={5088}, journal={Science}, publisher={American Association for the Advancement of Science (AAAS)}, author={Yu, Hongtao and Rosen, Michael K. and Shin, Tae Bum and Seidel-Dugan, Cynthia and Brugge, Joan S. and Schreiber, Stuart L.}, year={1992}, month=dec, pages={1665–1668} }