View source for 4azm


==Human epidermal fatty acid-binding protein (FABP5) in complex with the inhibitor BMS-309413==
<StructureSection load='4azm' size='340' side='right' caption='[[4azm]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4azm]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AZM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AZM FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=T4B:((2-(5-ETHYL-3,4-DIPHENYL-1H-PYRAZOL-1-YL)-3-BIPHENYLYL)OXY)ACETIC+ACID'>T4B</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1b56|1b56]], [[1jjj|1jjj]], [[4azn|4azn]], [[4azo|4azo]], [[4azp|4azp]], [[4azq|4azq]], [[4azr|4azr]]</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=4azm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4azm OCA], [http://pdbe.org/4azm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4azm RCSB], [http://www.ebi.ac.uk/pdbsum/4azm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4azm ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/FABP5_HUMAN FABP5_HUMAN]] High specificity for fatty acids. Highest affinity for C18 chain length. Decreasing the chain length or introducing double bonds reduces the affinity. May be involved in keratinocyte differentiation. 
<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 4azm" style="background-color:#fffaf0;"></div>

==See Also==
*[[Fatty acid-binding protein|Fatty acid-binding protein]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Human]]
[[Category: Deutsch, D]]
[[Category: Kaczocha, M]]
[[Category: Li, H]]
[[Category: Ojima, I]]
[[Category: Sanson, B]]
[[Category: Sun, J]]
[[Category: Wang, T]]
[[Category: Beta-barrel]]
[[Category: Beta-clamshell]]
[[Category: Domain swapping]]
[[Category: Endocannabinoid]]
[[Category: Lipid binding protein]]
[[Category: Lipid carrier protein]]