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1koz

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[[Image:1koz.gif|left|200px]]
[[Image:1koz.gif|left|200px]]
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{{Structure
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{{STRUCTURE_1koz| PDB=1koz | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1koz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1koz OCA], [http://www.ebi.ac.uk/pdbsum/1koz PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1koz RCSB]</span>
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'''SOLUTION STRUCTURE OF OMEGA-GRAMMOTOXIN SIA'''
'''SOLUTION STRUCTURE OF OMEGA-GRAMMOTOXIN SIA'''
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==About this Structure==
==About this Structure==
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1KOZ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KOZ OCA].
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1KOZ is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KOZ OCA].
==Reference==
==Reference==
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[[Category: Takahashi, H.]]
[[Category: Takahashi, H.]]
[[Category: Takeuchi, K.]]
[[Category: Takeuchi, K.]]
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[[Category: cystine knot]]
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[[Category: Cystine knot]]
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[[Category: toxin]]
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[[Category: Toxin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:51:33 2008''
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Revision as of 19:59, 2 May 2008

Template:STRUCTURE 1koz

SOLUTION STRUCTURE OF OMEGA-GRAMMOTOXIN SIA


Overview

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

1KOZ is a Single protein structure. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Fri May 2 22:59:58 2008

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