2p0f: Difference between revisions
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'''ArhGAP9 PH domain in complex with Ins(1,3,5)P3''' | {{Structure | ||
|PDB= 2p0f |SIZE=350|CAPTION= <scene name='initialview01'>2p0f</scene>, resolution 1.91Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</scene> | |||
|ACTIVITY= | |||
|GENE= ARHGAP9 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |||
}} | |||
'''ArhGAP9 PH domain in complex with Ins(1,3,5)P3''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2P0F is a [ | 2P0F is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P0F OCA]. | ||
==Reference== | ==Reference== | ||
Non-canonical interaction of phosphoinositides with pleckstrin homology domains of Tiam1 and ArhGAP9., Ceccarelli DF, Blasutig IM, Goudreault M, Li Z, Ruston J, Pawson T, Sicheri F, J Biol Chem. 2007 May 4;282(18):13864-74. Epub 2007 Mar 5. PMID:[http:// | Non-canonical interaction of phosphoinositides with pleckstrin homology domains of Tiam1 and ArhGAP9., Ceccarelli DF, Blasutig IM, Goudreault M, Li Z, Ruston J, Pawson T, Sicheri F, J Biol Chem. 2007 May 4;282(18):13864-74. Epub 2007 Mar 5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17339315 17339315] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: protein-phosphoinositide complex]] | [[Category: protein-phosphoinositide complex]] | ||
''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 18:06:56 2008'' | ||
Revision as of 19:06, 20 March 2008
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| , resolution 1.91Å | |||||||
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| Ligands: | |||||||
| Gene: | ARHGAP9 (Homo sapiens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ArhGAP9 PH domain in complex with Ins(1,3,5)P3
OverviewOverview
Pleckstrin homology (PH) domains are phosphoinositide (PI)-binding modules that target proteins to membrane surfaces. Here we define a family of PH domain proteins, including Tiam1 and ArhGAP9, that demonstrates specificity for PI(4,5)P(2), as well as for PI(3,4,5)P(3) and PI(3,4)P(2), the products of PI 3-kinase. These PH domain family members utilize a non-canonical phosphoinositide binding pocket related to that employed by beta-spectrin. Crystal structures of the PH domain of ArhGAP9 in complex with the headgroups of Ins(1,3,4)P(3), Ins(1,4,5)P(3), and Ins(1,3,5)P(3) reveal how two adjacent phosphate positions in PI(3,4)P(2), PI(4,5)P(2), and PI(3,4,5)P(3) are accommodated through flipped conformations of the bound phospholipid. We validate the non-canonical site of phosphoinositide interaction by showing that binding pocket mutations, which disrupt phosphoinositide binding in vitro, also disrupt membrane localization of Tiam1 in cells. We posit that the diversity in PI interaction modes displayed by PH domains contributes to their versatility of use in biological systems.
About this StructureAbout this Structure
2P0F is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Non-canonical interaction of phosphoinositides with pleckstrin homology domains of Tiam1 and ArhGAP9., Ceccarelli DF, Blasutig IM, Goudreault M, Li Z, Ruston J, Pawson T, Sicheri F, J Biol Chem. 2007 May 4;282(18):13864-74. Epub 2007 Mar 5. PMID:17339315
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