View source for 4azq


==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]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4azq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4AZQ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4azq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4azq OCA], [https://pdbe.org/4azq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4azq RCSB], [https://www.ebi.ac.uk/pdbsum/4azq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4azq ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FABP5_MOUSE FABP5_MOUSE] High specificity for fatty acids. Highest affinity for C18 chain length (By similarity).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
In 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<ref>PMID:24531463</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4azq" style="background-color:#fffaf0;"></div>

==See Also==
*[[Fatty acid-binding protein 3D structures|Fatty acid-binding protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Deutsch D]]
[[Category: Kaczocha M]]
[[Category: Li H]]
[[Category: Ojima I]]
[[Category: Sanson B]]
[[Category: Sun J]]
[[Category: Wang T]]