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Solution Structure of the SH3 Domain of Src and Identification of Its Ligand-Binding Site
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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Cited by
Combining evolutionary information and neural networks to predict protein secondary structure
Rost, B., & Sander, C. (1994) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.340190108 · Cited by 1,452
Structure and regulation of Src family kinases
Boggon, T. J., & Eck, M. J. (2004) · Oncogene · doi:10.1038/sj.onc.1208081 · Cited by 712
Src kinases as therapeutic targets for cancer
Kim, L. C., Song, L., & Haura, E. B. (2009) · Nature Reviews Clinical Oncology · doi:10.1038/nrclinonc.2009.129 · Cited by 700
Pawson, T., & Schlessingert, J. (1993) · Current Biology · doi:10.1016/0960-9822(93)90350-w · Cited by 688
Feng, S., Chen, J. K., Yu, H., Simon, J. A., & Schreiber, S. L. (1994) · Science · doi:10.1126/science.7526465 · Cited by 687
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Metadata
- Authors
- Yu, H., Rosen, M. K., Shin, T. B., Seidel-Dugan, C., Brugge, J. S., & Schreiber, S. L.
- Venue
- Science
- Published
- 1992-12-04
- Volume
- 258
- Issue
- 5088
- Pages
- 1665-1668
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1975898157
- Cited by
- 326
- References
- 0
- FWCI
- 16.67
- Type
- journal article
- Language
- en
- Open access
- closed
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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. https://doi.org/10.1126/science.1280858
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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