1tr6: Difference between revisions

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[[Image:1tr6.png|left|200px]]
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{{STRUCTURE_1tr6|  PDB=1tr6  |  SCENE=  }}  
{{STRUCTURE_1tr6|  PDB=1tr6  |  SCENE=  }}  
===NMR solution structure of omega-conotoxin [K10]GVIA, a cyclic cysteine knot peptide===
===NMR solution structure of omega-conotoxin [K10]GVIA, a cyclic cysteine knot peptide===
{{ABSTRACT_PUBMED_15166237}}


 
==Function==
<!--
[[http://www.uniprot.org/uniprot/CXO6_CONGE CXO6_CONGE]] Omega-conotoxins act at presynaptic membranes, they bind and block voltage-gated calcium channels (Cav).  
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{{ABSTRACT_PUBMED_15166237}}


==About this Structure==
==About this Structure==
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==Reference==
==Reference==
<ref group="xtra">PMID:015166237</ref><references group="xtra"/>
<ref group="xtra">PMID:015166237</ref><references group="xtra"/><references/>
[[Category: Conus geographus]]
[[Category: Conus geographus]]
[[Category: Adams, D J.]]
[[Category: Adams, D J.]]

Revision as of 08:43, 23 April 2014

Template:STRUCTURE 1tr6

NMR solution structure of omega-conotoxin [K10]GVIA, a cyclic cysteine knot peptide

Template:ABSTRACT PUBMED 15166237

Function

[CXO6_CONGE] Omega-conotoxins act at presynaptic membranes, they bind and block voltage-gated calcium channels (Cav).

About this Structure

1tr6 is a 1 chain structure with sequence from Conus geographus. Full experimental information is available from OCA.

Reference

  1. Mould J, Yasuda T, Schroeder CI, Beedle AM, Doering CJ, Zamponi GW, Adams DJ, Lewis RJ. The alpha2delta auxiliary subunit reduces affinity of omega-conotoxins for recombinant N-type (Cav2.2) calcium channels. J Biol Chem. 2004 Aug 13;279(33):34705-14. Epub 2004 May 27. PMID:15166237 doi:10.1074/jbc.M310848200

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