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| {{STRUCTURE_2p0d| PDB=2p0d | SCENE= }} | | {{STRUCTURE_2p0d| PDB=2p0d | SCENE= }} |
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| '''ArhGAP9 PH domain in complex with Ins(1,4,5)P3'''
| | ===ArhGAP9 PH domain in complex with Ins(1,4,5)P3=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17339315}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17339315 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17339315}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Pleckstrin homology domain]] | | [[Category: Pleckstrin homology domain]] |
| [[Category: Protein-phosphoinositide complex]] | | [[Category: Protein-phosphoinositide complex]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 12:03:22 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:42:18 2008'' |
