2SHP

TYROSINE PHOSPHATASE SHP-2

2SHP の概要

• エントリーDOI: 10.2210/pdb2shp/pdb
• 分子名称: SHP-2, DODECANE-TRIMETHYLAMINE (3 entities in total)
• 機能のキーワード: tyrosine phosphatase, insulin signaling, sh2 protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: Q06124
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 120820.73

構造登録者

Hof, P.,Pluskey, S.,Dhe-Paganon, S.,Eck, M.J.,Shoelson, S.E. (登録日: 1997-12-01, 公開日: 1999-02-16, 最終更新日: 2024-04-03)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2 Å)