1fgy

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[[Image:1fgy.jpg|left|200px]]
[[Image:1fgy.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1fgy |SIZE=350|CAPTION= <scene name='initialview01'>1fgy</scene>, resolution 1.5&Aring;
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The line below this paragraph, containing "STRUCTURE_1fgy", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=4IP:INOSITOL-(1,3,4,5)-TETRAKISPHOSPHATE'>4IP</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1fgy| PDB=1fgy | SCENE= }}
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|RELATEDENTRY=[[1fgz|1FGZ]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fgy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fgy OCA], [http://www.ebi.ac.uk/pdbsum/1fgy PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fgy RCSB]</span>
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}}
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'''GRP1 PH DOMAIN WITH INS(1,3,4,5)P4'''
'''GRP1 PH DOMAIN WITH INS(1,3,4,5)P4'''
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[[Category: Lambright, D G.]]
[[Category: Lambright, D G.]]
[[Category: Lietzke, S E.]]
[[Category: Lietzke, S E.]]
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[[Category: ph domain]]
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[[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 Sun Mar 30 20:22:41 2008''
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Revision as of 13:18, 2 May 2008

Image:1fgy.jpg

Template:STRUCTURE 1fgy

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 Fri May 2 16:18:47 2008

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OCA

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