1fgz: Difference between revisions
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[[Image:1fgz.jpg|left|200px]] | [[Image:1fgz.jpg|left|200px]] | ||
'''GRP1 PH DOMAIN (UNLIGANDED)''' | {{Structure | ||
|PDB= 1fgz |SIZE=350|CAPTION= <scene name='initialview01'>1fgz</scene>, resolution 2.05Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''GRP1 PH DOMAIN (UNLIGANDED)''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1FGZ is a [ | 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== | ||
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 11:08:57 2008'' | ||
Revision as of 09:08, 20 March 2008
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| 1fgz, resolution 2.05Å | |||||||||||||
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| Ligands: | SO4 | ||||||||||||
| 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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