Revealing mechanisms for SH2 domain mediated regulation of the protein tyrosine phosphatase SHP-2

Structure. 1998 Mar 15;6(3):249-54. doi: 10.1016/s0969-2126(98)00027-6.

Abstract

The crystal structure of the protein tyrosine phosphatase SHP-2 reveals the mechanism of auto-inhibition of phosphatase activity by its SH2 domains. Phosphotyrosine peptide stimulation of the phosphatase activity, resulting from peptide binding to the N-terminal SH2 domain, is linked to conformational changes within the protein, including an unprecedented allosteric transition of the N-terminal SH2 domain.

Publication types

  • Review

MeSH terms

  • Enzyme Activation
  • Intracellular Signaling Peptides and Proteins
  • Models, Molecular
  • Protein Conformation
  • Protein Tyrosine Phosphatase, Non-Receptor Type 11
  • Protein Tyrosine Phosphatase, Non-Receptor Type 6
  • Protein Tyrosine Phosphatases / chemistry*
  • Protein Tyrosine Phosphatases / metabolism*
  • SH2 Domain-Containing Protein Tyrosine Phosphatases
  • Signal Transduction
  • src Homology Domains*

Substances

  • Intracellular Signaling Peptides and Proteins
  • Protein Tyrosine Phosphatase, Non-Receptor Type 11
  • Protein Tyrosine Phosphatase, Non-Receptor Type 6
  • Protein Tyrosine Phosphatases
  • SH2 Domain-Containing Protein Tyrosine Phosphatases