4azp: Difference between revisions
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==Murine epidermal fatty acid-binding protein (FABP5) in complex with the endocannabinoid anandamide== | |||
<StructureSection load='4azp' size='340' side='right'caption='[[4azp]], [[Resolution|resolution]] 2.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4azp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AZP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AZP 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]] 2.1Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A9M:N-(2-HYDROXYETHYL)ICOSANAMIDE'>A9M</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=4azp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4azp OCA], [https://pdbe.org/4azp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4azp RCSB], [https://www.ebi.ac.uk/pdbsum/4azp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4azp ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/FABP5_MOUSE FABP5_MOUSE] High specificity for fatty acids. Highest affinity for C18 chain length (By similarity). | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
In addition to binding intracellular fatty acids, fatty-acid-binding proteins (FABPs) have recently been reported to also transport the endocannabinoids anandamide (AEA) and 2-arachidonoylglycerol (2-AG), arachidonic acid derivatives that function as neurotransmitters and mediate a diverse set of physiological and psychological processes. To understand how the endocannabinoids bind to FABPs, the crystal structures of FABP5 in complex with AEA, 2-AG and the inhibitor BMS-309403 were determined. These ligands are shown to interact primarily with the substrate-binding pocket via hydrophobic interactions as well as a common hydrogen bond to the Tyr131 residue. This work advances our understanding of FABP5-endocannabinoid interactions and may be useful for future efforts in the development of small-molecule inhibitors to raise endocannabinoid levels. | |||
Crystallographic study of FABP5 as an intracellular endocannabinoid transporter.,Sanson B, Wang T, Sun J, Wang L, Kaczocha M, Ojima I, Deutsch D, Li H Acta Crystallogr D Biol Crystallogr. 2014 Feb;70(Pt 2):290-8. doi:, 10.1107/S1399004713026795. Epub 2014 Jan 29. PMID:24531463<ref>PMID:24531463</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4azp" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Fatty acid-binding protein 3D structures|Fatty acid-binding protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mus musculus]] | |||
[[Category: Deutsch D]] | |||
[[Category: Kaczocha M]] | |||
[[Category: Li H]] | |||
[[Category: Ojima I]] | |||
[[Category: Sanson B]] | |||
[[Category: Sun J]] | |||
[[Category: Wang T]] | |||
Latest revision as of 14:39, 20 December 2023
Murine epidermal fatty acid-binding protein (FABP5) in complex with the endocannabinoid anandamideMurine epidermal fatty acid-binding protein (FABP5) in complex with the endocannabinoid anandamide
Structural highlights
FunctionFABP5_MOUSE High specificity for fatty acids. Highest affinity for C18 chain length (By similarity). Publication Abstract from PubMedIn addition to binding intracellular fatty acids, fatty-acid-binding proteins (FABPs) have recently been reported to also transport the endocannabinoids anandamide (AEA) and 2-arachidonoylglycerol (2-AG), arachidonic acid derivatives that function as neurotransmitters and mediate a diverse set of physiological and psychological processes. To understand how the endocannabinoids bind to FABPs, the crystal structures of FABP5 in complex with AEA, 2-AG and the inhibitor BMS-309403 were determined. These ligands are shown to interact primarily with the substrate-binding pocket via hydrophobic interactions as well as a common hydrogen bond to the Tyr131 residue. This work advances our understanding of FABP5-endocannabinoid interactions and may be useful for future efforts in the development of small-molecule inhibitors to raise endocannabinoid levels. Crystallographic study of FABP5 as an intracellular endocannabinoid transporter.,Sanson B, Wang T, Sun J, Wang L, Kaczocha M, Ojima I, Deutsch D, Li H Acta Crystallogr D Biol Crystallogr. 2014 Feb;70(Pt 2):290-8. doi:, 10.1107/S1399004713026795. Epub 2014 Jan 29. PMID:24531463[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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