1FGY

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

Summary for 1FGY

• Entry DOI: 10.2210/pdb1fgy/pdb
• Related: 1FGZ
• Descriptor: GRP1, INOSITOL-(1,3,4,5)-TETRAKISPHOSPHATE (3 entities in total)
• Functional Keywords: ph domain, signaling protein
• Biological source: Mus musculus (house mouse)
• Total number of polymer chains: 1
• Total formula weight: 15619.04

Authors

Lietzke, S.E.,Bose, S.,Cronin, T.,Klarlund, J.,Chawla, A.,Czech, M.P.,Lambright, D.G. (deposition date: 2000-07-29, release date: 2000-08-23, Last modification date: 2024-11-06)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.5 Å)