6l1d
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of human StAR-related lipid transfer protein 4== | |
| + | <StructureSection load='6l1d' size='340' side='right'caption='[[6l1d]], [[Resolution|resolution]] 1.95Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6l1d]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6L1D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6L1D FirstGlance]. <br> | ||
| + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6l1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6l1d OCA], [http://pdbe.org/6l1d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6l1d RCSB], [http://www.ebi.ac.uk/pdbsum/6l1d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6l1d ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/STAR4_HUMAN STAR4_HUMAN]] Involved in the intracellular transport of cholesterol. Binds cholesterol or other sterols.<ref>PMID:18403318</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The steroidogenic acute regulatory protein (StAR)-related lipid transfer domain-4 (STARD4) is a sterol-binding protein that is involved in cholesterol homeostasis by intracellular sterol transport. In this work, we determined the crystal structures of human STARD4 and its Omega1-loop mutant in apo forms at 1.95 and 1.7A resolutions, respectively. The structure of human STARD4 displays a conserved alpha-helix/beta-grip fold containing a deep hydrophobic pocket. The Omega1-loop which serves as a lid for the hydrophobic pocket has a closed conformation. The shape of the sterol-binding cavity in the closed form is not complementary to accommodate cholesterol, suggesting that a conformational change of the Omega1-loop is essential for sterol binding. The human STARD4 displayed sterol transfer activity between liposomes, and the mutations in the Omega1-loop and the hydrophobic wall abolished the transfer activity. This study confirms the structural conservation of the STARD4 subfamily proteins and the flexibility of the Omega1-loop and helix alpha4 required for sterol transport. | ||
| - | + | Structural analysis of human sterol transfer protein STARD4.,Tan L, Tong J, Chun C, Im YJ Biochem Biophys Res Commun. 2019 Oct 10. pii: S0006-291X(19)31941-2. doi:, 10.1016/j.bbrc.2019.10.054. PMID:31607485<ref>PMID:31607485</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6l1d" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Im, Y J]] | ||
| + | [[Category: Tong, J]] | ||
| + | [[Category: Cholesterol]] | ||
| + | [[Category: Lipid transfer protein]] | ||
| + | [[Category: Lipid transport]] | ||
| + | [[Category: Stard4]] | ||
| + | [[Category: Sterol]] | ||
| + | [[Category: Transport protein]] | ||
Revision as of 09:05, 30 October 2019
Structure of human StAR-related lipid transfer protein 4
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