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6gn5
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==CRYSTAL STRUCTURE OF HUMAN GRAMD1C START DOMAIN== | |
| - | + | <StructureSection load='6gn5' size='340' side='right'caption='[[6gn5]], [[Resolution|resolution]] 1.41Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[6gn5]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GN5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GN5 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr> | |
| - | [[Category: | + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=6gn5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gn5 OCA], [http://pdbe.org/6gn5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6gn5 RCSB], [http://www.ebi.ac.uk/pdbsum/6gn5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6gn5 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/ASTRC_HUMAN ASTRC_HUMAN]] Cholesterol transporter that mediates non-vesicular transport of cholesterol from the plasma membrane (PM) to the endoplasmic reticulum (ER) (By similarity). Contains unique domains for binding cholesterol and the PM, thereby serving as a molecular bridge for the transfer of cholesterol from the PM to the ER (By similarity). Plays a crucial role in cholesterol homeostasis and has the unique ability to localize to the PM based on the level of membrane cholesterol (By similarity). In lipid-poor conditions localizes to the ER membrane and in response to excess cholesterol in the PM is recruited to the endoplasmic reticulum-plasma membrane contact sites (EPCS) which is mediated by the GRAM domain (By similarity). At the EPCS, the sterol-binding VASt/ASTER domain binds to the cholesterol in the PM and facilitates its transfer from the PM to ER (By similarity).[UniProtKB:Q8CI52] | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Friese, A]] | [[Category: Friese, A]] | ||
| - | [[Category: Vetter, I | + | [[Category: Vetter, I R]] |
| + | [[Category: Alpha/beta helix grip fold]] | ||
| + | [[Category: Lipid transport]] | ||
| + | [[Category: Sterol binding]] | ||
Revision as of 05:53, 19 June 2019
CRYSTAL STRUCTURE OF HUMAN GRAMD1C START DOMAIN
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