Structures of SH2 and SH3 domains. Current opinion in structural biology 1993, 3:828-837

John Kuriyan, David Cowburn

Research output: Contribution to journalArticle

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Abstract

SH2 and SH3 domains are small protein modules of about 100 and 60 amino acids, respectively, that are found in many proteins involved in intracellular signal transduction. SH2 and SH3 domains mediate protein-protein interactions and modulate enzyme activity by their ability to bind to specific phosphorylated tyrosine residues or proline-rich sequences, respectively. The recent determination of the three-dimensional structures of several SH2 and SH3 domains has led to considerable progress in understanding their mechanism of action, and these structures are the focus of this review.

Original languageEnglish (US)
Pages (from-to)828-837
Number of pages10
JournalCurrent Opinion in Structural Biology
Volume3
Issue number6
DOIs
Publication statusPublished - 1993

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ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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