4omj
From Proteopedia
(Difference between revisions)
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- | ''' | + | ==Crystal structure of SPF bound to 2,3-oxidosqualene== |
- | + | <StructureSection load='4omj' size='340' side='right' caption='[[4omj]], [[Resolution|resolution]] 1.60Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[4omj]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OMJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OMJ FirstGlance]. <br> | |
- | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2TX:(3S)-2,2-DIMETHYL-3-[(3E,7E,11E,15E)-3,7,12,16,20-PENTAMETHYLHENICOSA-3,7,11,15,19-PENTAEN-1-YL]OXIRANE'>2TX</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |
- | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1olm|1olm]], [[1o6u|1o6u]], [[4omk|4omk]]</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=4omj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4omj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4omj RCSB], [http://www.ebi.ac.uk/pdbsum/4omj PDBsum]</span></td></tr> | |
- | [[ | + | </table> |
- | [[ | + | == Function == |
- | [[ | + | [[http://www.uniprot.org/uniprot/S14L2_HUMAN S14L2_HUMAN]] Carrier protein. Binds to some hydrophobic molecules and promotes their transfer between the different cellular sites. Binds with high affinity to alpha-tocopherol. Also binds with a weaker affinity to other tocopherols and to tocotrienols. May have a transcriptional activatory activity via its association with alpha-tocopherol. Probably recognizes and binds some squalene structure, suggesting that it may regulate cholesterol biosynthesis by increasing the transfer of squalene to a metabolic active pool in the cell. |
- | [[ | + | __TOC__ |
- | [[ | + | </StructureSection> |
[[Category: Cascella, M]] | [[Category: Cascella, M]] | ||
+ | [[Category: Christen, M]] | ||
+ | [[Category: Lamprakis, C]] | ||
+ | [[Category: Marcaida, M J]] | ||
+ | [[Category: Stocker, A]] | ||
+ | [[Category: 3-oxidosqualene]] | ||
+ | [[Category: Cholesterol synthesis]] | ||
+ | [[Category: Cral-trio domain]] | ||
+ | [[Category: Hydrophobic ligand transporter]] | ||
+ | [[Category: Sec14-like]] | ||
+ | [[Category: Squalene]] | ||
+ | [[Category: Transport protein]] |
Revision as of 12:57, 15 April 2015
Crystal structure of SPF bound to 2,3-oxidosqualene
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