1tr6

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[[Image:1tr6.png|left|200px]]
 
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{{STRUCTURE_1tr6| PDB=1tr6 | SCENE= }}
{{STRUCTURE_1tr6| PDB=1tr6 | SCENE= }}
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===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===
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{{ABSTRACT_PUBMED_15166237}}
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==Function==
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[[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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(as it appears on PubMed at http://www.pubmed.gov), where 15166237 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15166237}}
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==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:015166237</ref><references group="xtra"/>
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<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

Contents

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

  • 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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