1FGY

GRP1 PH DOMAIN WITH INS(1,3,4,5)P4

1FGY の概要

• エントリーDOI: 10.2210/pdb1fgy/pdb
• 関連するPDBエントリー: 1FGZ
• 分子名称: GRP1, INOSITOL-(1,3,4,5)-TETRAKISPHOSPHATE (3 entities in total)
• 機能のキーワード: ph domain, signaling protein
• 由来する生物種: Mus musculus (house mouse)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15619.04

構造登録者

Lietzke, S.E.,Bose, S.,Cronin, T.,Klarlund, J.,Chawla, A.,Czech, M.P.,Lambright, D.G. (登録日: 2000-07-29, 公開日: 2000-08-23, 最終更新日: 2024-11-06)

主引用文献

Lietzke, S.E.,Bose, S.,Cronin, T.,Klarlund, J.,Chawla, A.,Czech, M.P.,Lambright, D.G.
Structural basis of 3-phosphoinositide recognition by pleckstrin homology domains.
Mol.Cell, 6:385-394, 2000

PubMed Abstract: Lipid second messengers generated by phosphoinositide (PI) 3-kinases regulate diverse cellular functions through interaction with pleckstrin homology (PH) domains in modular signaling proteins. The PH domain of Grp1, a PI 3-kinase-activated exchange factor for Arf GTPases, selectively binds phosphatidylinositol 3,4,5-trisphosphate with high affinity. We have determined the structure of the Grp1 PH domain in the unliganded form and bound to inositol 1,3,4,5-tetraphosphate. A novel mode of phosphoinositide recognition involving a 20-residue insertion within the beta6/beta7 loop explains the unusually high specificity of the Grp1 PH domain and the promiscuous 3-phosphoinositide binding typical of several PH domains including that of protein kinase B. When compared to other PH domains, general determinants of 3-phosphoinositide recognition and specificity can be deduced.

PubMed: 10983985
DOI: 10.1016/S1097-2765(00)00038-1

実験手法

X-RAY DIFFRACTION (1.5 Å)