1fgy
From Proteopedia
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- | [[Image:1fgy.jpg|left|200px]] | + | [[Image:1fgy.jpg|left|200px]] |
- | + | ||
- | '''GRP1 PH DOMAIN WITH INS(1,3,4,5)P4''' | + | {{Structure |
+ | |PDB= 1fgy |SIZE=350|CAPTION= <scene name='initialview01'>1fgy</scene>, resolution 1.5Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=4IP:INOSITOL-(1,3,4,5)-TETRAKISPHOSPHATE'>4IP</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''GRP1 PH DOMAIN WITH INS(1,3,4,5)P4''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1FGY is a [ | + | 1FGY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FGY OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10983985 10983985] |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: ph domain]] | [[Category: ph domain]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:09:02 2008'' |
Revision as of 09:09, 20 March 2008
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, resolution 1.5Å | |||||||
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Coordinates: | save as pdb, mmCIF, xml |
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. 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 Thu Mar 20 11:09:02 2008
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