3v2n

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<StructureSection load='3v2n' size='340' side='right'caption='[[3v2n]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='3v2n' size='340' side='right'caption='[[3v2n]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3v2n]] 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=3V2N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3V2N FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3v2n]] is a 5 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=3V2N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3V2N FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1mz9|1mz9]], [[3v2p|3v2p]], [[3v2q|3v2q]], [[3v2r|3v2r]], [[3v2s|3v2s]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</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=3v2n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v2n OCA], [https://pdbe.org/3v2n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3v2n RCSB], [https://www.ebi.ac.uk/pdbsum/3v2n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3v2n ProSAT]</span></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=3v2n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v2n OCA], [https://pdbe.org/3v2n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3v2n RCSB], [https://www.ebi.ac.uk/pdbsum/3v2n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3v2n ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/COMP_MOUSE COMP_MOUSE] May play a role in the structural integrity of cartilage via its interaction with other extracellular matrix proteins such as the collagens and fibronectin. Can mediate the interaction of chondrocytes with the cartilage extracellular matrix through interaction with cell surface integrin receptors. Could play a role in the pathogenesis of osteoarthritis. Potent suppressor of apoptosis in both primary chondrocytes and transformed cells. Suppresses apoptosis by blocking the activation of caspase-3 and by inducing the IAP family of survival proteins (BIRC3, BIRC2, BIRC5 and XIAP). Essential for maintaining a vascular smooth muscle cells (VSMCs) contractile/differentiated phenotype under physiological and pathological stimuli. Maintains this phenotype of VSMCs by interacting with ITGA7 (By similarity).
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3v2n" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Lk3 transgenic mice]]
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[[Category: Mus musculus]]
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[[Category: Stetefeld, J]]
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[[Category: Stetefeld J]]
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[[Category: Coiled coil fatty acid]]
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[[Category: Protein binding]]
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[[Category: Storage]]
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Revision as of 14:15, 14 March 2024

COMPcc in complex with fatty acids

PDB ID 3v2n

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