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5hz5

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m (Protected "5hz5" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 5hz5 is ON HOLD
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==FABP5 in complex with 6-Chloro-4-phenyl-2-piperidin-1-yl-3-(1H-tetrazol-5-yl)-quinoline==
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<StructureSection load='5hz5' size='340' side='right' caption='[[5hz5]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5hz5]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HZ5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HZ5 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=65X:6-CHLORO-4-PHENYL-2-(PIPERIDIN-1-YL)-3-(1H-TETRAZOL-5-YL)QUINOLINE'>65X</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<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=5hz5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hz5 OCA], [http://pdbe.org/5hz5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hz5 RCSB], [http://www.ebi.ac.uk/pdbsum/5hz5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hz5 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[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.
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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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Authors: Ehler, A., Rudolph, M.G.
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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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Description: FABP5 in complex with 6-Chloro-4-phenyl-2-piperidin-1-yl-3-(1H-tetrazol-5-yl)-quinoline
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 5hz5" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Ehler, A]]
[[Category: Ehler, A]]
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[[Category: Rudolph, M.G]]
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[[Category: Rudolph, M G]]
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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: Transport]]

Revision as of 23:37, 25 January 2017

FABP5 in complex with 6-Chloro-4-phenyl-2-piperidin-1-yl-3-(1H-tetrazol-5-yl)-quinoline

5hz5, resolution 1.40Å

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