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1fgz

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(New page: 200px<br /><applet load="1fgz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fgz, resolution 2.05&Aring;" /> '''GRP1 PH DOMAIN (UNLI...)
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Revision as of 12:47, 20 November 2007

Image:1fgz.jpg

1fgz, resolution 2.05Å

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GRP1 PH DOMAIN (UNLIGANDED)

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

1FGZ is a Single protein structure of sequence from Mus musculus with SO4 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

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