5hz6

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<StructureSection load='5hz6' size='340' side='right'caption='[[5hz6]], [[Resolution|resolution]] 1.14&Aring;' scene=''>
<StructureSection load='5hz6' size='340' side='right'caption='[[5hz6]], [[Resolution|resolution]] 1.14&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5hz6]] 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=5HZ6 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5HZ6 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5hz6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HZ6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HZ6 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=65Y:6-CHLORO-2-ISOPROPYL-4-(3-ISOPROPYL-PHENYL)-QUINOLINE-3-CARBOXYLIC+ACID'>65Y</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.14&#8491;</td></tr>
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<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>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=65Y:6-CHLORO-2-ISOPROPYL-4-(3-ISOPROPYL-PHENYL)-QUINOLINE-3-CARBOXYLIC+ACID'>65Y</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5hz6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hz6 OCA], [http://pdbe.org/5hz6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hz6 RCSB], [http://www.ebi.ac.uk/pdbsum/5hz6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hz6 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5hz6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hz6 OCA], [https://pdbe.org/5hz6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hz6 RCSB], [https://www.ebi.ac.uk/pdbsum/5hz6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hz6 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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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[https://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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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Dual inhibition of fatty acid binding proteins 4 and 5 (FABP4 and FABP5) is expected to provide beneficial effects on a number of metabolic parameters such as insulin sensitivity and blood glucose levels and should protect against atherosclerosis. Starting from a FABP4 selective focused screening hit, biostructure information was used to modulate the selectivity profile in the desired way and to design potent dual FABP4/5 inhibitors with good selectivity against FABP3. With very good pharmacokinetic properties and no major safety alerts, compound 12 was identified as a suitable tool compound for further in vivo investigations.
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Design and synthesis of selective, dual fatty acid binding protein 4 and 5 inhibitors.,Kuhne H, Obst-Sander U, Kuhn B, Conte A, Ceccarelli SM, Neidhart W, Rudolph MG, Ottaviani G, Gasser R, So SS, Li S, Zhang X, Gao L, Myers M Bioorg Med Chem Lett. 2016 Oct 15;26(20):5092-5097. doi:, 10.1016/j.bmcl.2016.08.071. Epub 2016 Aug 22. PMID:27658368<ref>PMID:27658368</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5hz6" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Fatty acid-binding protein 3D structures|Fatty acid-binding protein 3D structures]]
*[[Fatty acid-binding protein 3D structures|Fatty acid-binding protein 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Ehler, A]]
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[[Category: Ehler A]]
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[[Category: Rudolph, M G]]
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[[Category: Rudolph MG]]
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[[Category: Cytoplasm]]
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[[Category: Fatty acid binding protein]]
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[[Category: Lipid binding protein]]
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[[Category: Lipid-binding]]
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[[Category: Protein binding]]
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[[Category: Ro6806346_refmac]]
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[[Category: Transport protein]]
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Current revision

FABP4 in complex with 6-Chloro-2-isopropyl-4-(3-isopropyl-phenyl)-quinoline-3-carboxylic acid

PDB ID 5hz6

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