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New page: left|200px<br /><applet load="1koz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1koz" /> '''SOLUTION STRUCTURE OF OMEGA-GRAMMOTOXIN SIA'...
 
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[[Image:1koz.gif|left|200px]]<br /><applet load="1koz" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1koz" />
'''SOLUTION STRUCTURE OF OMEGA-GRAMMOTOXIN SIA'''<br />


==Overview==
==SOLUTION STRUCTURE OF OMEGA-GRAMMOTOXIN SIA==
omega-Grammotoxin SIA (GrTx) is a 36 amino acid residue protein toxin from, spider venom that inhibits P/Q and N-type voltage-gated Ca(2+) channels by, modifying voltage-dependent gating. We determined the three-dimensional, structure of GrTx using NMR spectroscopy. The toxin adopts an "inhibitor, cystine knot" motif composed of two beta-strands (Leu19-Cys21 and, Cys30-Trp32) and a beta-bulge (Trp6, Gly7-Cys30) with a +2x, -1 topology, which are connected by four chain reversals. Although GrTx was originally, identified as an inhibitor of voltage-gated Ca(2+) channel, it also binds, to K(+) channels with lower affinity. A similar cross-reaction was, observed for Hanatoxin1 (HaTx), which binds to the voltage-sensing domains, of K(+) and Ca(2+) channels with different affinities. A detailed, comparison of the GrTx and HaTx structures identifies a conserved face, containing a large hydrophobic patch surrounded by positively charged, residues. The slight differences in the surface shape, which result from, the orientation of the surface aromatic residues and/or the distribution, of the charged residues, may explain the differences in the binding, affinity of these gating modifiers with different voltage-gated ion, channels.
<StructureSection load='1koz' size='340' side='right'caption='[[1koz]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1koz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Grammostola_rosea Grammostola rosea]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KOZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KOZ 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=1koz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1koz OCA], [https://pdbe.org/1koz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1koz RCSB], [https://www.ebi.ac.uk/pdbsum/1koz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1koz ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/WGRTX_GRARO WGRTX_GRARO] Inhibits P/Q- (Cav2.1/CACNA1A) and N-type (Cav2.2/CACNA1B) voltage-gated calcium channel by modifying voltage-dependent gating. It selectively and reversibly blocks the calcium channels coupled to glutamate release. Also inhibits potassium channels (Kv2.1/KCNB1) with lower affinity.<ref>PMID:21740921</ref> <ref>PMID:8394998</ref> <ref>PMID:8848236</ref> <ref>PMID:9415720</ref> <ref>PMID:9671721</ref>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
omega-Grammotoxin SIA (GrTx) is a 36 amino acid residue protein toxin from spider venom that inhibits P/Q and N-type voltage-gated Ca(2+) channels by modifying voltage-dependent gating. We determined the three-dimensional structure of GrTx using NMR spectroscopy. The toxin adopts an "inhibitor cystine knot" motif composed of two beta-strands (Leu19-Cys21 and Cys30-Trp32) and a beta-bulge (Trp6, Gly7-Cys30) with a +2x, -1 topology, which are connected by four chain reversals. Although GrTx was originally identified as an inhibitor of voltage-gated Ca(2+) channel, it also binds to K(+) channels with lower affinity. A similar cross-reaction was observed for Hanatoxin1 (HaTx), which binds to the voltage-sensing domains of K(+) and Ca(2+) channels with different affinities. A detailed comparison of the GrTx and HaTx structures identifies a conserved face containing a large hydrophobic patch surrounded by positively charged residues. The slight differences in the surface shape, which result from the orientation of the surface aromatic residues and/or the distribution of the charged residues, may explain the differences in the binding affinity of these gating modifiers with different voltage-gated ion channels.


==About this Structure==
Solution structure of omega-grammotoxin SIA, a gating modifier of P/Q and N-type Ca(2+) channel.,Takeuchi K, Park E, Lee C, Kim J, Takahashi H, Swartz K, Shimada I J Mol Biol. 2002 Aug 16;321(3):517-26. PMID:12162963<ref>PMID:12162963</ref>
1KOZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KOZ OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Solution structure of omega-grammotoxin SIA, a gating modifier of P/Q and N-type Ca(2+) channel., Takeuchi K, Park E, Lee C, Kim J, Takahashi H, Swartz K, Shimada I, J Mol Biol. 2002 Aug 16;321(3):517-26. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12162963 12162963]
</div>
[[Category: Single protein]]
<div class="pdbe-citations 1koz" style="background-color:#fffaf0;"></div>
[[Category: Kim, J.I.]]
== References ==
[[Category: Lee, C.W.]]
<references/>
[[Category: Park, E.J.]]
__TOC__
[[Category: Shimada, I.]]
</StructureSection>
[[Category: Swartz, K.J.]]
[[Category: Grammostola rosea]]
[[Category: Takahashi, H.]]
[[Category: Large Structures]]
[[Category: Takeuchi, K.]]
[[Category: Kim JI]]
[[Category: cystine knot]]
[[Category: Lee CW]]
[[Category: toxin]]
[[Category: Park EJ]]
 
[[Category: Shimada I]]
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:32:19 2007''
[[Category: Swartz KJ]]
[[Category: Takahashi H]]
[[Category: Takeuchi K]]
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