2SHP

TYROSINE PHOSPHATASE SHP-2

Summary for 2SHP

• Entry DOI: 10.2210/pdb2shp/pdb
• Descriptor: SHP-2, DODECANE-TRIMETHYLAMINE (3 entities in total)
• Functional Keywords: tyrosine phosphatase, insulin signaling, sh2 protein
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: Q06124
• Total number of polymer chains: 2
• Total formula weight: 120820.73

Authors

Hof, P.,Pluskey, S.,Dhe-Paganon, S.,Eck, M.J.,Shoelson, S.E. (deposition date: 1997-12-01, release date: 1999-02-16, Last modification date: 2024-04-03)

Primary citation

Hof, P.,Pluskey, S.,Dhe-Paganon, S.,Eck, M.J.,Shoelson, S.E.
Crystal structure of the tyrosine phosphatase SHP-2.
Cell(Cambridge,Mass.), 92:441-450, 1998

PubMed Abstract: The structure of the SHP-2 tyrosine phosphatase, determined at 2.0 angstroms resolution, shows how its catalytic activity is regulated by its two SH2 domains. In the absence of a tyrosine-phosphorylated binding partner, the N-terminal SH2 domain binds the phosphatase domain and directly blocks its active site. This interaction alters the structure of the N-SH2 domain, disrupting its phosphopeptide-binding cleft. Conversely, interaction of the N-SH2 domain with phosphopeptide disrupts its phosphatase recognition surface. Thus, the N-SH2 domain is a conformational switch; it either binds and inhibits the phosphatase, or it binds phosphoproteins and activates the enzyme. Recognition of bisphosphorylated ligands by the tandem SH2 domains is an integral element of this switch; the C-terminal SH2 domain contributes binding energy and specificity, but it does not have a direct role in activation.

PubMed: 9491886
DOI: 10.1016/S0092-8674(00)80938-1

Experimental method

X-RAY DIFFRACTION (2 Å)