3fr5

<StructureSection load='3fr5' size='340' side='right' caption='[[3fr5]], [[Resolution|resolution]] 2.20&Aring;' scene=''>

<table><tr><td colspan='2'>[[3fr5]] is a 1 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=3FR5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3FR5 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=I4A:5-(3-CARBAMOYLBENZYL)-5,6,7,8,9,10-HEXAHYDROCYCLOHEPTA[B]INDOLE-4-CARBOXYLIC+ACID'>I4A</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3fr2|3fr2]], [[3fr4|3fr4]]</td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FABP4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3fr5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fr5 OCA], [http://pdbe.org/3fr5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3fr5 RCSB], [http://www.ebi.ac.uk/pdbsum/3fr5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3fr5 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/FABP4_HUMAN FABP4_HUMAN]] Lipid transport protein in adipocytes. Binds both long chain fatty acids and retinoic acid. Delivers long-chain fatty acids and retinoic acid to their cognate receptors in the nucleus (By similarity).

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== Publication Abstract from PubMed ==

Small molecule inhibitors of adipocyte fatty-acid binding protein (A-FABP) have gained renewed interest following the recent publication of pharmacologically beneficial effects of such inhibitors. Despite the potential utility of selective A-FABP inhibitors within the fields of metabolic disease, inflammation and atherosclerosis, there are few examples of useful A-FABP inhibitors in the public domain. Herein, we describe the optimization of N-benzyl-tetrahydrocarbazole derivatives through the use of co-crystal structure guided medicinal chemistry efforts. This led to the identification of a potent and selective class of A-FABP inhibitors as illustrated by N-benzyl-hexahydrocyclohepta[b]indole 30.

N-Benzyl-indolo carboxylic acids: Design and synthesis of potent and selective adipocyte fatty-acid binding protein (A-FABP) inhibitors.,Barf T, Lehmann F, Hammer K, Haile S, Axen E, Medina C, Uppenberg J, Svensson S, Rondahl L, Lundback T Bioorg Med Chem Lett. 2009 Mar 15;19(6):1745-8. Epub 2009 Jan 30. PMID:19217286<ref>PMID:19217286</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 3fr5" style="background-color:#fffaf0;"></div>

*[[Fatty acid-binding protein|Fatty acid-binding protein]]

[[Category: Human]]

[[Category: Axen, E]]

[[Category: Barf, T]]

[[Category: Haile, S]]

[[Category: Hammer, K]]

[[Category: Lehmann, F]]

[[Category: Medina, C]]

[[Category: Rondahl, L]]

[[Category: Svensson, S]]

[[Category: Uppenberg, J]]

[[Category: Transport]]