Critical residues in an SH3 domain from Sem-5 suggest a mechanism for proline-rich peptide recognition
Author:
Publisher
Springer Science and Business Media LLC
Subject
Molecular Biology,Structural Biology
Link
http://www.nature.com/articles/nsb0494-221.pdf
Reference26 articles.
1. C. elegans cell-signalling gene sem-5 encodes a protein with SH2 and SH3 domains
2. An SH3-SH2-SH3 protein is required for p21Ras1 activation and binds to sevenless and Sos proteins in vitro
3. A Drosophila SH2-SH3 adaptor protein implicated in coupling the sevenless tyrosine kinase to an activator of Ras guanine nucleotide exchange, Sos
4. Association of Sos Ras exchange protein with Grb2 is implicated in tyrosine kinase signal transduction and transformation
5. Repression of c-fos promoter by MyoD on muscle cell differentiation
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