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7cyz
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 7cyz is ON HOLD Authors: Dong, X. Description: The structure of human ORP3 OSBP-related domain Category: Unreleased Structures [[Category: Dong...) |
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| - | '''Unreleased structure''' | ||
| - | The | + | ==The structure of human ORP3 OSBP-related domain== |
| + | <StructureSection load='7cyz' size='340' side='right'caption='[[7cyz]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7cyz]] is a 2 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=7CYZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CYZ FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAF:S-DIMETHYLARSINOYL-CYSTEINE'>CAF</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7cyz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cyz OCA], [https://pdbe.org/7cyz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cyz RCSB], [https://www.ebi.ac.uk/pdbsum/7cyz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cyz ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/OSBL3_HUMAN OSBL3_HUMAN] Phosphoinositide-binding protein which associates with both cell and endoplasmic reticulum (ER) membranes (PubMed:16143324). Can bind to the ER membrane protein VAPA and recruit VAPA to plasma membrane sites, thus linking these intracellular compartments (PubMed:25447204). The ORP3-VAPA complex stimulates RRAS signaling which in turn attenuates integrin beta-1 (ITGB1) activation at the cell surface (PubMed:18270267, PubMed:25447204). With VAPA, may regulate ER morphology (PubMed:16143324). Has a role in regulation of the actin cytoskeleton, cell polarity and cell adhesion (PubMed:18270267). Binds to phosphoinositides with preference for PI(3,4)P2 and PI(3,4,5)P3 (PubMed:16143324). Also binds 25-hydroxycholesterol and cholesterol (PubMed:17428193).<ref>PMID:16143324</ref> <ref>PMID:17428193</ref> <ref>PMID:18270267</ref> <ref>PMID:25447204</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Oxysterol-binding protein (OSBP) and its related protein (ORP) constitute a conserved family of lipid transfer proteins (LTPs). ORPs have been implicated as intracellular lipid exchanger and sensor in recent years, which regulate the lipid homeostasis and signal pathway. OSBP-related protein 3 plays key role in controlling cell adhesion and migration and could be developed as the drug target for cancer therapy. Here, we report the crystal structures of human ORP3 ORD to 2.1 A and ORD-PI4P complex to 3.2 A. The binding assay in vitro confirms the ORP3 has the capability of PI4P binding. This study further verifies that the PI4P is the common ligand of all ORPs and ORPs should be the lipid exchanger in membrane contact sites(MCS). | ||
| - | + | The crystal structure of ORP3 reveals the conservative PI4P binding pattern.,Dong X, Wang Z, Ye S, Zhang R Biochem Biophys Res Commun. 2020 Sep 3;529(4):1005-1010. doi:, 10.1016/j.bbrc.2020.06.090. Epub 2020 Jul 30. PMID:32819557<ref>PMID:32819557</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Dong | + | <div class="pdbe-citations 7cyz" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Dong X]] | ||
Current revision
The structure of human ORP3 OSBP-related domain
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