1fgy
From Proteopedia
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GRP1 PH DOMAIN WITH INS(1,3,4,5)P4
Overview
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.
About this Structure
1FGY is a Single protein structure of sequence from Mus musculus with 4IP as ligand. Full crystallographic information is available from OCA.
Reference
Structural basis of 3-phosphoinositide recognition by pleckstrin homology domains., Lietzke SE, Bose S, Cronin T, Klarlund J, Chawla A, Czech MP, Lambright DG, Mol Cell. 2000 Aug;6(2):385-94. PMID:10983985
Page seeded by OCA on Tue Nov 20 14:55:06 2007
Categories: Mus musculus | Single protein | Bose, S. | Chawla, A. | Cronin, T. | Czech, M.P. | Klarlund, J. | Lambright, D.G. | Lietzke, S.E. | 4IP | Ph domain
