3v2n
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | + | ==COMPcc in complex with fatty acids== | |
| - | === | + | <StructureSection load='3v2n' size='340' side='right' caption='[[3v2n]], [[Resolution|resolution]] 1.80Å' scene=''> |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[3v2n]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V2N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3V2N FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1mz9|1mz9]], [[3v2p|3v2p]], [[3v2q|3v2q]], [[3v2r|3v2r]], [[3v2s|3v2s]]</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=3v2n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v2n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3v2n RCSB], [http://www.ebi.ac.uk/pdbsum/3v2n PDBsum]</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> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
| - | [[Category: Stetefeld, J | + | [[Category: Stetefeld, J]] |
[[Category: Coiled coil fatty acid]] | [[Category: Coiled coil fatty acid]] | ||
[[Category: Protein binding]] | [[Category: Protein binding]] | ||
[[Category: Storage]] | [[Category: Storage]] | ||
Revision as of 07:43, 15 February 2015
COMPcc in complex with fatty acids
| |||||||||||
