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3v2q
From Proteopedia
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| - | [[Image:3v2q.jpg|left|200px]] | ||
| - | + | ==COMPcc in complex with fatty acids== | |
| + | <StructureSection load='3v2q' size='340' side='right'caption='[[3v2q]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3v2q]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V2Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3V2Q FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3v2n|3v2n]], [[3v2p|3v2p]], [[3v2r|3v2r]], [[3v2s|3v2s]]</div></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=3v2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v2q OCA], [https://pdbe.org/3v2q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3v2q RCSB], [https://www.ebi.ac.uk/pdbsum/3v2q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3v2q ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | BACKGROUND: COMPcc forms a pentameric left-handed coiled coil that is known to bind hydrophilic signaling molecules such as vitamin D(3), and vitamin A. PRINCIPAL FINDINGS: In an integrated approach we reveal the unique binding properties of COMPcc for saturated and unsaturated fatty acids. Our observations suggest that residues Met33 (gating pore), Thr40/Asn41 (water chamber) and Gln54 (electrostatic trap) are key elements for the binding of fatty acids by COMPcc. In addition, this work characterizes the binding of various fatty acids to COMPcc using fluorescence spectroscopy. Our findings reveal a binding trend within the hydrophobic channel of COMPcc, namely, that is driven by length of the methylene tail and incorporation of unsaturation. CONCLUSION/SIGNIFICANCE: The unique binding properties imply that COMPcc may be involved in signalling functions in which hydrophilic ligands are involved. The pentameric channel is a unique carrier for lipophilic compounds. This opens the exciting possibility that COMPcc could be developed as a targeted drug delivery system. | ||
| - | + | The pentameric channel of COMPcc in complex with different fatty acids.,MacFarlane AA, Orriss G, Okun N, Meier M, Klonisch T, Khajehpour M, Stetefeld J PLoS One. 2012;7(11):e48130. doi: 10.1371/journal.pone.0048130. Epub 2012 Nov 2. PMID:23133613<ref>PMID:23133613</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | == | + | </div> |
| - | + | <div class="pdbe-citations 3v2q" style="background-color:#fffaf0;"></div> | |
| - | [[Category: | + | == References == |
| - | [[Category: Stetefeld, J | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Lk3 transgenic mice]] | ||
| + | [[Category: Stetefeld, J]] | ||
[[Category: Coiled coil palmitic acid]] | [[Category: Coiled coil palmitic acid]] | ||
[[Category: Protein binding]] | [[Category: Protein binding]] | ||
[[Category: Storage]] | [[Category: Storage]] | ||
Current revision
COMPcc in complex with fatty acids
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