2p0f
From Proteopedia
(New page: 200px<br /> <applet load="2p0f" size="450" color="white" frame="true" align="right" spinBox="true" caption="2p0f, resolution 1.91Å" /> '''ArhGAP9 PH domain i...) |
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| - | [[Image:2p0f. | + | [[Image:2p0f.jpg|left|200px]]<br /><applet load="2p0f" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="2p0f, resolution 1.91Å" /> | caption="2p0f, resolution 1.91Å" /> | ||
'''ArhGAP9 PH domain in complex with Ins(1,3,5)P3'''<br /> | '''ArhGAP9 PH domain in complex with Ins(1,3,5)P3'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2P0F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with PO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2P0F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=PO4:'>PO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P0F OCA]. |
==Reference== | ==Reference== | ||
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[[Category: protein-phosphoinositide complex]] | [[Category: protein-phosphoinositide complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:19:47 2008'' |
Revision as of 13:19, 23 January 2008
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ArhGAP9 PH domain in complex with Ins(1,3,5)P3
Overview
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 Structure
2P0F is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
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:17339315
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