6l1d: Difference between revisions

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'''Unreleased structure'''


The entry 6l1d is ON HOLD until Paper Publication
==Structure of human StAR-related lipid transfer protein 4==
<StructureSection load='6l1d' size='340' side='right'caption='[[6l1d]], [[Resolution|resolution]] 1.95&Aring;' 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.


Authors:  
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>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</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]]
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