4lkt: Difference between revisions
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==Crystal Structure of Human Epidermal Fatty Acid Binding Protein (FABP5) in Complex with Linoleic Acid== | ==Crystal Structure of Human Epidermal Fatty Acid Binding Protein (FABP5) in Complex with Linoleic Acid== | ||
<StructureSection load='4lkt' size='340' side='right' caption='[[4lkt]], [[Resolution|resolution]] 2.57Å' scene=''> | <StructureSection load='4lkt' size='340' side='right'caption='[[4lkt]], [[Resolution|resolution]] 2.57Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4lkt]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4lkt]] is a 4 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=4LKT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LKT FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EIC:LINOLEIC+ACID'>EIC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TAR:D(-)-TARTARIC+ACID'>TAR</scene> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EIC:LINOLEIC+ACID'>EIC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TAR:D(-)-TARTARIC+ACID'>TAR</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=4lkt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lkt OCA], [https://pdbe.org/4lkt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lkt RCSB], [https://www.ebi.ac.uk/pdbsum/4lkt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lkt ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://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. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 20: | Line 18: | ||
</div> | </div> | ||
<div class="pdbe-citations 4lkt" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4lkt" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Fatty acid-binding protein 3D structures|Fatty acid-binding protein 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Armstrong EH]] | ||
[[Category: | [[Category: Ortlund EA]] | ||
Revision as of 14:07, 14 December 2022
Crystal Structure of Human Epidermal Fatty Acid Binding Protein (FABP5) in Complex with Linoleic AcidCrystal Structure of Human Epidermal Fatty Acid Binding Protein (FABP5) in Complex with Linoleic Acid
Structural highlights
FunctionFABP5_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. Publication Abstract from PubMedFatty acid-binding proteins (FABPs) are a widely expressed group of calycins that play a well established role in solubilizing cellular fatty acids. Recent studies, however, have recast FABPs as active participants in vital lipid-signaling pathways. FABP5, like its family members, displays a promiscuous ligand binding profile, capable of interacting with numerous long chain fatty acids of varying degrees of saturation. Certain "activating" fatty acids induce the protein's cytoplasmic to nuclear translocation, stimulating PPARbeta/delta transactivation; however, the rules that govern this process remain unknown. Using a range of structural and biochemical techniques, we show that both linoleic and arachidonic acid elicit FABP5's translocation by permitting allosteric communication between the ligand-sensing beta2 loop and a tertiary nuclear localization signal within the alpha-helical cap of the protein. Furthermore, we show that more saturated, nonactivating fatty acids inhibit nuclear localization signal formation by destabilizing this activation loop, thus implicating FABP5 specifically in cis-bonded, polyunsaturated fatty acid signaling. Structural basis for ligand regulation of the fatty acid-binding protein 5, peroxisome proliferator-activated receptor beta/delta (FABP5-PPARbeta/delta) signaling pathway.,Armstrong EH, Goswami D, Griffin PR, Noy N, Ortlund EA J Biol Chem. 2014 May 23;289(21):14941-54. doi: 10.1074/jbc.M113.514646. Epub, 2014 Apr 1. PMID:24692551[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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