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4xwg
From Proteopedia
(Difference between revisions)
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| - | ''' | + | ==Crystal Structure of LCAT (C31Y) in complex with Fab1== |
| - | + | <StructureSection load='4xwg' size='340' side='right' caption='[[4xwg]], [[Resolution|resolution]] 2.65Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4xwg]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XWG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XWG FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |
| - | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4xx1|4xx1]]</td></tr> | |
| - | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphatidylcholine--sterol_O-acyltransferase Phosphatidylcholine--sterol O-acyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.43 2.3.1.43] </span></td></tr> | |
| - | [[Category: | + | <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=4xwg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xwg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4xwg RCSB], [http://www.ebi.ac.uk/pdbsum/4xwg PDBsum]</span></td></tr> |
| - | [[Category: Piper, D | + | </table> |
| - | [[Category: Romanow, W | + | == Disease == |
| - | [[Category: Walker, N | + | [[http://www.uniprot.org/uniprot/LCAT_HUMAN LCAT_HUMAN]] Fish-eye disease;Familial LCAT deficiency. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. |
| - | [[Category: | + | == Function == |
| + | [[http://www.uniprot.org/uniprot/LCAT_HUMAN LCAT_HUMAN]] Central enzyme in the extracellular metabolism of plasma lipoproteins. Synthesized mainly in the liver and secreted into plasma where it converts cholesterol and phosphatidylcholines (lecithins) to cholesteryl esters and lysophosphatidylcholines on the surface of high and low density lipoproteins (HDLs and LDLs). The cholesterol ester is then transported back to the liver. Has a preference for plasma 16:0-18:2 or 18:O-18:2 phosphatidylcholines. Also produced in the brain by primary astrocytes, and esterifies free cholesterol on nascent APOE-containing lipoproteins secreted from glia and influences cerebral spinal fluid (CSF) APOE- and APOA1 levels. Together with APOE and the cholesterol transporter ABCA1, plays a key role in the maturation of glial-derived, nascent lipoproteins. Required for remodeling high-density lipoprotein particles into their spherical forms.<ref>PMID:10722751</ref> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Phosphatidylcholine--sterol O-acyltransferase]] | ||
| + | [[Category: Piper, D E]] | ||
| + | [[Category: Romanow, W G]] | ||
| + | [[Category: Thibault, S T]] | ||
| + | [[Category: Walker, N P.C]] | ||
| + | [[Category: A-b hydrolase complex]] | ||
| + | [[Category: Acyl transferase]] | ||
| + | [[Category: Esterase]] | ||
| + | [[Category: Hydrolase-immune system complex]] | ||
Revision as of 14:51, 29 July 2015
Crystal Structure of LCAT (C31Y) in complex with Fab1
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