2PNB

STRUCTURE OF AN SH2 DOMAIN OF THE P85 ALPHA SUBUNIT OF PHOSPHATIDYLINOSITOL-3-OH KINASE

2PNB の概要

• エントリーDOI: 10.2210/pdb2pnb/pdb
• 分子名称: PHOSPHATIDYLINOSITOL 3-KINASE P85-ALPHA SUBUNIT N-TERMINAL SH2 DOMAIN (1 entity in total)
• 機能のキーワード: signalling protein
• 由来する生物種: Bos taurus (cattle)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12147.63

構造登録者

Booker, G.W.,Breeze, A.L.,Downing, A.K.,Panayotou, G.,Gout, I.,Waterfield, M.D.,Campbell, I.D. (登録日: 1992-06-30, 公開日: 1994-01-31, 最終更新日: 2024-05-01)

主引用文献

Booker, G.W.,Breeze, A.L.,Downing, A.K.,Panayotou, G.,Gout, I.,Waterfield, M.D.,Campbell, I.D.
Structure of an SH2 domain of the p85 alpha subunit of phosphatidylinositol-3-OH kinase.
Nature, 358:684-687, 1992

PubMed Abstract: Receptor protein-tyrosine kinases, through phosphorylation of specific tyrosine residues, generate high-affinity binding sites which direct assembly of multienzyme signalling complexes. Many of these signalling proteins, including phospholipase C gamma, GTPase-activating protein and phosphatidylinositol-3-OH kinase, contain src-homology 2 (SH2) domains, which bind with high affinity and specificity to tyrosine-phosphorylated sequences. The critical role played by SH2 domains in signalling has been highlighted by recent studies showing that mutation of specific phosphorylation sites on the platelet-derived growth factor receptor impair its association with phosphatidylinositol-3-OH kinase, preventing growth factor-induced mitogenesis. Here we report the solution structure of an isolated SH2 domain from the 85K regulatory subunit of phosphatidylinositol-3-OH kinase, determined using multidimensional nuclear magnetic resonance spectroscopy. The structure is characterized by a central region of beta-sheet flanked by two alpha-helices, with a highly flexible loop close to functionally important residues previously identified by site-directed mutagenesis.

PubMed: 1323062
DOI: 10.1038/358684a0

実験手法

SOLUTION NMR