View source for 1fu3


==THREE-DIMENSIONAL STRUCTURE IN SOLUTION OF THE SODIUM CHANNEL AGONIST/ANTAGONIST DELTA-CONOTOXIN TXVIA==
<StructureSection load='1fu3' size='340' side='right'caption='[[1fu3]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1fu3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Conus_textile Conus textile]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FU3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FU3 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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=1fu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fu3 OCA], [https://pdbe.org/1fu3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fu3 RCSB], [https://www.ebi.ac.uk/pdbsum/1fu3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fu3 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/O16A_CONTE O16A_CONTE] Delta-conotoxins bind to site 6 of voltage-gated sodium channels (Nav) and inhibit the inactivation process. Binding of this toxin is strongly calcium-dependent but not voltage-dependent. The binding site is most likely on the extracellular side of the sodium channel. Binds receptor sites on both mollusk and rat central nervous system, but despite its high affinity binding to rat sodium channel, it has no functional effect in vivo and in vitro on it. Has also no effect on Gambusia fish. Is important in mollusk for the paralysis of the prey. Upon injection of the peptide, a subordinate lobster assumes an exaggerated dominant posture (of a 'King-Kong' lobster!).<ref>PMID:1761058</ref> <ref>PMID:2706261</ref> <ref>PMID:8261090</ref> <ref>PMID:8300586</ref> 
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== Publication Abstract from PubMed ==
The three-dimensional solution structure of delta-conotoxin TxVIA, a 27-mer peptide agonist/antagonist of sodium channels, was determined by two-dimensional (1)H NMR spectroscopy with simulated annealing calculations. A total of 20 converged structures of delta-conotoxin TxVIA were obtained on the basis of 360 distance constraints obtained from nuclear Overhauser effect connectivities, 28 torsion angle constraints, and 27 constraints associated with hydrogen bonds and disulfide bonds. The atomic root mean square difference about the averaged coordinate positions is 0.35 +/- 0.07 A for the backbone atoms (N, C(alpha), C) and 0.98 +/- 0.14 A for all heavy atoms of the entire peptide. The molecular structure of delta-conotoxin TxVIA is composed of a short triple-stranded antiparallel beta-sheet. The overall beta-sheet topology is +2x, -1, which is the same as those for other conotoxins. However, the three-dimensional structure of delta-conotoxin TxVIA has an unusual hydrophobic patch on one side of the molecule, which may play an important role in the sodium channel binding. These results provide a molecular basis for understanding the mechanism of sodium channel modulation through the toxin-channel interaction and insight into the discrimination of different ion channels.

Three-dimensional solution structure of the sodium channel agonist/antagonist delta-conotoxin TxVIA.,Kohno T, Sasaki T, Kobayashi K, Fainzilber M, Sato K J Biol Chem. 2002 Sep 27;277(39):36387-91. Epub 2002 Jul 26. PMID:12145313<ref>PMID:12145313</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Conus textile]]
[[Category: Large Structures]]
[[Category: Fainzilber M]]
[[Category: Kohno T]]
[[Category: Sasaki T]]
[[Category: Sato K]]