3p6e: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
 ==Human adipocyte lipid-binding protein FABP4 in complex with 3-(4-methoxyphenyl) propionic acid==
-<StructureSection load='3p6e' size='340' side='right' caption='[[3p6e]], [[Resolution|resolution]] 1.08&Aring;' scene=''>
+<StructureSection load='3p6e' size='340' side='right'caption='[[3p6e]], [[Resolution|resolution]] 1.08&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3p6e]] 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=3P6E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3P6E FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3p6e]] 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=3P6E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3P6E FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZGC:3-(4-METHOXYPHENYL)PROPANOIC+ACID'>ZGC</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.08&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3p6c|3p6c]], [[3p6d|3p6d]], [[3p6f|3p6f]], [[3p6g|3p6g]], [[3p6h|3p6h]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZGC:3-(4-METHOXYPHENYL)PROPANOIC+ACID'>ZGC</scene></td></tr>
-<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>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3p6e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3p6e OCA], [https://pdbe.org/3p6e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3p6e RCSB], [https://www.ebi.ac.uk/pdbsum/3p6e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3p6e ProSAT]</span></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=3p6e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3p6e OCA], [http://pdbe.org/3p6e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3p6e RCSB], [http://www.ebi.ac.uk/pdbsum/3p6e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3p6e 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).
+[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 ==
-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.
-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>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3p6e" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Fatty acid-binding protein|Fatty acid-binding protein]]
+*[[Fatty acid-binding protein 3D structures|Fatty acid-binding protein 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
-[[Category: Gonzalez, J M]]
+[[Category: Large Structures]]
-[[Category: Pozharski, E]]
+[[Category: Gonzalez JM]]
-[[Category: Beta barrel]]
+[[Category: Pozharski E]]
-[[Category: Fatty acid binding protein]]
-[[Category: Lipid binding protein]]
-[[Category: Lipocalin]]