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Cell Rep. 2013 Apr 25;3(4):1293-305. doi: 10.1016/j.celrep.2013.03.001. Epub 2013 Mar 28.

The SH2 domain interaction landscape.

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1
Department of Biology, University of Rome Tor Vergata, I-00133 Rome, Italy.

Abstract

Members of the SH2 domain family modulate signal transduction by binding to short peptides containing phosphorylated tyrosines. Each domain displays a distinct preference for the sequence context of the phosphorylated residue. We have developed a high-density peptide chip technology that allows for probing of the affinity of most SH2 domains for a large fraction of the entire complement of tyrosine phosphopeptides in the human proteome. Using this technique, we have experimentally identified thousands of putative SH2-peptide interactions for more than 70 different SH2 domains. By integrating this rich data set with orthogonal context-specific information, we have assembled an SH2-mediated probabilistic interaction network, which we make available as a community resource in the PepspotDB database. A predicted dynamic interaction between the SH2 domains of the tyrosine phosphatase SHP2 and the phosphorylated tyrosine in the extracellular signal-regulated kinase activation loop was validated by experiments in living cells.

PMID:
23545499
PMCID:
PMC4110347
DOI:
10.1016/j.celrep.2013.03.001
[Indexed for MEDLINE]
Free PMC Article
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