4azq: Difference between revisions
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==Murine epidermal fatty acid-binding protein (FABP5) in complex with the endocannabinoid 2-arachidonoylglycerol== | ==Murine epidermal fatty acid-binding protein (FABP5) in complex with the endocannabinoid 2-arachidonoylglycerol== | ||
<StructureSection load='4azq' size='340' side='right' caption='[[4azq]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='4azq' size='340' side='right'caption='[[4azq]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4azq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AZQ OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[4azq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AZQ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=4AZQ FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=G2A:2-HYDROXY-1-(HYDROXYMETHYL)ETHYL+ICOSANOATE'>G2A</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=G2A:2-HYDROXY-1-(HYDROXYMETHYL)ETHYL+ICOSANOATE'>G2A</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4azr|4azr]], [[4azn|4azn]], [[4azo|4azo]], [[4azp|4azp]], [[4azm|4azm]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4azr|4azr]], [[4azn|4azn]], [[4azo|4azo]], [[4azp|4azp]], [[4azm|4azm]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=4azq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4azq OCA], [http://pdbe.org/4azq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4azq RCSB], [http://www.ebi.ac.uk/pdbsum/4azq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4azq ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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==See Also== | ==See Also== | ||
*[[Fatty acid-binding protein|Fatty acid-binding protein]] | *[[Fatty acid-binding protein 3D structures|Fatty acid-binding protein 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Lk3 transgenic mice]] | [[Category: Lk3 transgenic mice]] | ||
[[Category: Deutsch, D]] | [[Category: Deutsch, D]] |
Revision as of 11:13, 4 November 2020
Murine epidermal fatty acid-binding protein (FABP5) in complex with the endocannabinoid 2-arachidonoylglycerolMurine epidermal fatty acid-binding protein (FABP5) in complex with the endocannabinoid 2-arachidonoylglycerol
Structural highlights
Function[FABP5_MOUSE] High specificity for fatty acids. Highest affinity for C18 chain length (By similarity). Publication Abstract from PubMedIn addition to binding intracellular fatty acids, fatty-acid-binding proteins (FABPs) have recently been reported to also transport the endocannabinoids anandamide (AEA) and 2-arachidonoylglycerol (2-AG), arachidonic acid derivatives that function as neurotransmitters and mediate a diverse set of physiological and psychological processes. To understand how the endocannabinoids bind to FABPs, the crystal structures of FABP5 in complex with AEA, 2-AG and the inhibitor BMS-309403 were determined. These ligands are shown to interact primarily with the substrate-binding pocket via hydrophobic interactions as well as a common hydrogen bond to the Tyr131 residue. This work advances our understanding of FABP5-endocannabinoid interactions and may be useful for future efforts in the development of small-molecule inhibitors to raise endocannabinoid levels. Crystallographic study of FABP5 as an intracellular endocannabinoid transporter.,Sanson B, Wang T, Sun J, Wang L, Kaczocha M, Ojima I, Deutsch D, Li H Acta Crystallogr D Biol Crystallogr. 2014 Feb;70(Pt 2):290-8. doi:, 10.1107/S1399004713026795. Epub 2014 Jan 29. PMID:24531463[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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