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1fgz

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[[Image:1fgz.jpg|left|200px]]<br /><applet load="1fgz" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1fgz.jpg|left|200px]]
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caption="1fgz, resolution 2.05&Aring;" />
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'''GRP1 PH DOMAIN (UNLIGANDED)'''<br />
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{{Structure
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|PDB= 1fgz |SIZE=350|CAPTION= <scene name='initialview01'>1fgz</scene>, resolution 2.05&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''GRP1 PH DOMAIN (UNLIGANDED)'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1FGZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FGZ OCA].
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1FGZ 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=1FGZ OCA].
==Reference==
==Reference==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=10983985 10983985]
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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]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:38:33 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:08:57 2008''

Revision as of 09:08, 20 March 2008


PDB ID 1fgz

Drag the structure with the mouse to rotate
, resolution 2.05Å
Ligands:
Coordinates: save as pdb, mmCIF, xml



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. 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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