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3p6c

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==Human adipocyte lipid-binding protein FABP4 in complex with citric acid==
==Human adipocyte lipid-binding protein FABP4 in complex with citric acid==
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<StructureSection load='3p6c' size='340' side='right' caption='[[3p6c]], [[Resolution|resolution]] 1.25&Aring;' scene=''>
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<StructureSection load='3p6c' size='340' side='right'caption='[[3p6c]], [[Resolution|resolution]] 1.25&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3p6c]] 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=3P6C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3P6C FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3p6c]] 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=3P6C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3P6C 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=CIT:CITRIC+ACID'>CIT</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]] 1.25&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3p6d|3p6d]], [[3p6e|3p6e]], [[3p6f|3p6f]], [[3p6g|3p6g]], [[3p6h|3p6h]]</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=CIT:CITRIC+ACID'>CIT</scene></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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3p6c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3p6c OCA], [https://pdbe.org/3p6c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3p6c RCSB], [https://www.ebi.ac.uk/pdbsum/3p6c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3p6c ProSAT]</span></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=3p6c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3p6c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3p6c RCSB], [http://www.ebi.ac.uk/pdbsum/3p6c PDBsum]</span></td></tr>
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</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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Inhibition of human adipocyte fatty-acid binding protein (FABP4) has been proposed as a treatment for type 2 diabetes, fatty liver disease and atherosclerosis. However, FABP4 displays a naturally low selectivity towards hydrophobic ligands, leading to the possibility of side effects arising from cross-inhibition of other FABP isoforms. In a search for structural determinants of ligand-binding selectivity, the binding of FABP4 towards a group of small molecules structurally related to the nonsteroidal anti-inflammatory drug ibuprofen was analyzed through X-ray crystallography. Several specific hydrophobic interactions are shown to enhance the binding affinities of these compounds, whereas an aromatic edge-to-face interaction is proposed to determine the conformation of bound ligands, highlighting the importance of aromatic interactions in hydrophobic environments.
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Structural analysis of ibuprofen binding to human adipocyte fatty-acid binding protein (FABP4).,Gonzalez JM, Fisher SZ Acta Crystallogr F Struct Biol Commun. 2015 Feb;71(Pt 2):163-70. doi:, 10.1107/S2053230X14027897. Epub 2015 Jan 28. PMID:25664790<ref>PMID:25664790</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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==See Also==
==See Also==
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*[[Fatty acid-binding protein|Fatty acid-binding protein]]
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*[[Fatty acid-binding protein 3D structures|Fatty acid-binding protein 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Gonzalez, J M]]
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[[Category: Large Structures]]
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[[Category: Pozharski, E]]
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[[Category: Gonzalez JM]]
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[[Category: Beta barrel]]
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[[Category: Pozharski E]]
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[[Category: Fatty acid binding protein]]
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[[Category: Lipid binding protein]]
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[[Category: Lipocalin]]
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Current revision

Human adipocyte lipid-binding protein FABP4 in complex with citric acid

PDB ID 3p6c

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