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1tt3

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[[Image:1tt3.png|left|200px]]
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==NMR soulution structure of omega-conotoxin [K10]MVIIA==
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<StructureSection load='1tt3' size='340' side='right' caption='[[1tt3]], [[NMR_Ensembles_of_Models | 22 NMR models]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1tt3]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TT3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TT3 FirstGlance]. <br>
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</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1omg|1omg]], [[1mvj|1mvj]], [[1dw4|1dw4]], [[1ttk|1ttk]]</td></tr>
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<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=1tt3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tt3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1tt3 RCSB], [http://www.ebi.ac.uk/pdbsum/1tt3 PDBsum]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Neurotransmitter release from preganglionic parasympathetic neurons is resistant to inhibition by selective antagonists of L-, N-, P/Q-, R-, and T-type calcium channels. In this study, the effects of different omega-conotoxins from genus Conus were investigated on current flow-through cloned voltage-sensitive calcium channels expressed in Xenopus oocytes and nerve-evoked transmitter release from the intact preganglionic cholinergic nerves innervating the rat submandibular ganglia. Our results indicate that omega-conotoxin CVID from Conus catus inhibits a pharmacologically distinct voltage-sensitive calcium channel involved in neurotransmitter release, whereas omega-conotoxin MVIIA had no effect. omega-Conotoxin CVID and MVIIA inhibited depolarization-activated Ba(2+) currents recorded from oocytes expressing N-type but not L- or R-type calcium channels. High affinity inhibition of the CVID-sensitive calcium channel was enhanced when position 10 of the omega-conotoxin was occupied by the smaller residue lysine as found in CVID instead of an arginine as found in MVIIA. Given that relatively small differences in the sequence of the N-type calcium channel alpha(1B) subunit can influence omega-conotoxin access (Feng, Z. P., Hamid, J., Doering, C., Bosey, G. M., Snutch, T. P., and Zamponi, G. W. (2001) J. Biol. Chem. 276, 15728-15735), it is likely that the calcium channel in preganglionic nerve terminals targeted by CVID is a N-type (Ca(v)2.2) calcium channel variant.
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{{STRUCTURE_1tt3| PDB=1tt3 | SCENE= }}
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Omega-conotoxin CVID inhibits a pharmacologically distinct voltage-sensitive calcium channel associated with transmitter release from preganglionic nerve terminals.,Adams DJ, Smith AB, Schroeder CI, Yasuda T, Lewis RJ J Biol Chem. 2003 Feb 7;278(6):4057-62. Epub 2002 Nov 18. PMID:12441339<ref>PMID:12441339</ref>
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===NMR soulution structure of omega-conotoxin [K10]MVIIA===
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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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{{ABSTRACT_PUBMED_12441339}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[1tt3]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TT3 OCA].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:015166237</ref><references group="xtra"/>
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[[Category: Adams, D J.]]
[[Category: Adams, D J.]]
[[Category: Lewis, R J.]]
[[Category: Lewis, R J.]]

Revision as of 08:20, 8 October 2014

NMR soulution structure of omega-conotoxin [K10]MVIIA

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