2h8s: Difference between revisions

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[[Image:2h8s.png|left|200px]]
==Solution structure of alpha-conotoxin Vc1.1==
<StructureSection load='2h8s' size='340' side='right' caption='[[2h8s]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2h8s]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H8S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2H8S FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2h8s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h8s OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2h8s RCSB], [http://www.ebi.ac.uk/pdbsum/2h8s PDBsum]</span></td></tr>
<table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The alpha-conotoxin Vc1.1 is a small disulfide-bonded peptide currently in development as a treatment for neuropathic pain. This study describes the synthesis, determination of the disulfide connectivity, and the determination of the three-dimensional structure of Vc1.1 using NMR spectroscopy. Vc1.1 was shown to inhibit nicotine-evoked membrane currents in isolated bovine chromaffin cells in a concentration-dependent manner and preferentially targets peripheral nicotinic acetylcholine receptor (nAChR) subtypes over central subtypes. Specifically, Vc1.1 is selective for alpha3-containing nAChR subtypes. The three-dimensional structure of Vc1.1 comprises a small alpha-helix spanning residues Pro6 to Asp11 and is braced by the I-III, II-IV disulfide connectivity seen in other alpha-conotoxins. A comparison of the structure of Vc1.1 with other alpha-conotoxins, taken together with nAChR selectivity data, suggests that the conserved proline at position 6 is important for binding, whereas a number of residues in the C-terminal portion of the peptide contribute toward the selectivity. The structure reported here should open new opportunities for further development of Vc1.1 or analogues as analgesic agents.


{{STRUCTURE_2h8s|  PDB=2h8s  |  SCENE=  }}
The synthesis, structural characterization, and receptor specificity of the alpha-conotoxin Vc1.1.,Clark RJ, Fischer H, Nevin ST, Adams DJ, Craik DJ J Biol Chem. 2006 Aug 11;281(32):23254-63. Epub 2006 Jun 5. PMID:16754662<ref>PMID:16754662</ref>


===Solution structure of alpha-conotoxin Vc1.1===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_16754662}}
== References ==
 
<references/>
==About this Structure==
__TOC__
[[2h8s]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H8S OCA].
</StructureSection>
 
==Reference==
<ref group="xtra">PMID:016754662</ref><references group="xtra"/>
[[Category: Adams, D J.]]
[[Category: Adams, D J.]]
[[Category: Clark, R J.]]
[[Category: Clark, R J.]]
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