View source for 5d48


==Crystal Structure of FABP4 in complex with 3-{5-cyclopropyl-3-(3,5-dimethyl-1H-pyrazol-4-yl)-2-[3-(propan-2-yloxy) phenyl]-1H-indol-1-yl}propanoic acid==
<StructureSection load='5d48' size='340' side='right'caption='[[5d48]], [[Resolution|resolution]] 1.81&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5d48]] 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=5D48 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5D48 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.81&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=L96:3-{5-CYCLOPROPYL-3-(3,5-DIMETHYL-1H-PYRAZOL-4-YL)-2-[3-(PROPAN-2-YLOXY)PHENYL]-1H-INDOL-1-YL}PROPANOIC+ACID'>L96</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5d48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d48 OCA], [https://pdbe.org/5d48 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5d48 RCSB], [https://www.ebi.ac.uk/pdbsum/5d48 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5d48 ProSAT]</span></td></tr>
</table>
== Function ==
[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).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
X-ray crystal structural determination of FABP4 in complex with four inhibitors revealed the complex binding modes, and the resulting observations led to improvement of the inhibitory potency of FABP4 inhibitors. However, the detailed structure-activity relationship (SAR) could not be explained from these structural observations. For a more detailed understanding of the interactions between FABP4 and inhibitors, fragment molecular orbital analyses were performed. These analyses revealed that the total interfragment interaction energies of FABP4 and each inhibitor correlated with the ranking of the K i value for the four inhibitors. Furthermore, interactions between each inhibitor and amino acid residues in FABP4 were identified. The oxygen atom of Lys58 in FABP4 was found to be very important for strong interactions with FABP4. These results might provide useful information for the development of novel potent FABP4 inhibitors.

Interaction Analysis of FABP4 Inhibitors by X-ray Crystallography and Fragment Molecular Orbital Analysis.,Tagami U, Takahashi K, Igarashi S, Ejima C, Yoshida T, Takeshita S, Miyanaga W, Sugiki M, Tokumasu M, Hatanaka T, Kashiwagi T, Ishikawa K, Miyano H, Mizukoshi T ACS Med Chem Lett. 2016 Feb 16;7(4):435-9. doi: 10.1021/acsmedchemlett.6b00040., eCollection 2016 Apr 14. PMID:27096055<ref>PMID:27096055</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5d48" style="background-color:#fffaf0;"></div>

==See Also==
*[[Fatty acid-binding protein 3D structures|Fatty acid-binding protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Ejima C]]
[[Category: Hatanaka T]]
[[Category: Igarashi S]]
[[Category: Ishikawa K]]
[[Category: Kashiwagi T]]
[[Category: Miyanaga W]]
[[Category: Miyano H]]
[[Category: Mizukoshi T]]
[[Category: Sugiki M]]
[[Category: Tagami U]]
[[Category: Takahashi K]]
[[Category: Takeshita S]]
[[Category: Tokumasu M]]
[[Category: Yoshida T]]