5u78

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'''Unreleased structure'''
 
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The entry 5u78 is ON HOLD until Paper Publication
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==Crystal structure of ORP8 PH domain in P1211 space group==
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<StructureSection load='5u78' size='340' side='right'caption='[[5u78]], [[Resolution|resolution]] 1.98&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5u78]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5U78 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5U78 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.978&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5u78 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5u78 OCA], [https://pdbe.org/5u78 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5u78 RCSB], [https://www.ebi.ac.uk/pdbsum/5u78 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5u78 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/OSBL8_HUMAN OSBL8_HUMAN]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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ORP5 and ORP8, members of the oxysterol-binding protein (OSBP)-related proteins (ORP) family, are endoplasmic reticulum membrane proteins implicated in lipid trafficking. ORP5 and ORP8 are reported to localize to endoplasmic reticulum-plasma membrane junctions via binding to phosphatidylinositol-4-phosphate (PtdIns(4)P), and act as a PtdIns(4)P/phosphatidylserine counter exchanger between the endoplasmic reticulum and plasma membrane. Here we provide evidence that the pleckstrin homology domain of ORP5/8 via PtdIns(4,5)P 2, and not PtdIns(4)P binding mediates the recruitment of ORP5/8 to endoplasmic reticulum-plasma membrane contact sites. The OSBP-related domain of ORP8 can extract and transport multiple phosphoinositides in vitro, and knocking down both ORP5 and ORP8 in cells increases the plasma membrane level of PtdIns(4,5)P 2 with little effect on PtdIns(4)P. Overall, our data show, for the first time, that phosphoinositides other than PtdIns(4)P can also serve as co-exchangers for the transport of cargo lipids by ORPs.ORP5/8 are endoplasmic reticulum (ER) membrane proteins implicated in lipid trafficking that localize to ER-plasma membrane (PM) contacts and maintain membrane homeostasis. Here the authors show that PtdIns(4,5)P 2 plays a critical role in the targeting and function of ORP5/8 at the PM.
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Authors: Ghai, R., Yang, H.
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ORP5 and ORP8 bind phosphatidylinositol-4, 5-biphosphate (PtdIns(4,5)P 2) and regulate its level at the plasma membrane.,Ghai R, Du X, Wang H, Dong J, Ferguson C, Brown AJ, Parton RG, Wu JW, Yang H Nat Commun. 2017 Oct 2;8(1):757. doi: 10.1038/s41467-017-00861-5. PMID:28970484<ref>PMID:28970484</ref>
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Description: Crystal structure of ORP8 PH domain
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Yang, H]]
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<div class="pdbe-citations 5u78" style="background-color:#fffaf0;"></div>
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[[Category: Ghai, R]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Ghai R]]
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[[Category: Yang H]]

Current revision

Crystal structure of ORP8 PH domain in P1211 space group

PDB ID 5u78

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