5hz6: Difference between revisions

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'''Unreleased structure'''


The entry 5hz6 is ON HOLD  until Paper Publication
==FABP4 in complex with 6-Chloro-2-isopropyl-4-(3-isopropyl-phenyl)-quinoline-3-carboxylic acid==
<StructureSection load='5hz6' size='340' side='right' caption='[[5hz6]], [[Resolution|resolution]] 1.14&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5hz6]] is a 1 chain structure. 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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HZ6 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=65Y:6-CHLORO-2-ISOPROPYL-4-(3-ISOPROPYL-PHENYL)-QUINOLINE-3-CARBOXYLIC+ACID'>65Y</scene></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=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>
</table>
== Function ==
[[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).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


Authors: Ehler, A., Rudolph, M.G.
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>


Description: FABP4 in complex with 6-Chloro-2-isopropyl-4-(3-isopropyl-phenyl)-quinoline-3-carboxylic acid
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 5hz6" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Ehler, A]]
[[Category: Ehler, A]]
[[Category: Rudolph, M.G]]
[[Category: Rudolph, M G]]
[[Category: Cytoplasm]]
[[Category: Fatty acid binding protein]]
[[Category: Lipid binding protein]]
[[Category: Lipid-binding]]
[[Category: Protein binding]]
[[Category: Ro6806346_refmac]]
[[Category: Transport protein]]
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