1fgy

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{{STRUCTURE_1fgy| PDB=1fgy | SCENE= }}
{{STRUCTURE_1fgy| PDB=1fgy | SCENE= }}
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'''GRP1 PH DOMAIN WITH INS(1,3,4,5)P4'''
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===GRP1 PH DOMAIN WITH INS(1,3,4,5)P4===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 10983985 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10983985}}
==About this Structure==
==About this Structure==
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[[Category: Lietzke, S E.]]
[[Category: Lietzke, S E.]]
[[Category: Ph domain]]
[[Category: Ph domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:18:47 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:14:02 2008''

Revision as of 00:14, 1 July 2008

Image:1fgy.png

Template:STRUCTURE 1fgy

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

Template:ABSTRACT PUBMED 10983985

About this Structure

1FGY is a Single protein structure of sequence from Mus musculus. 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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