1koz

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(New page: 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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'''SOLUTION STRUCTURE OF OMEGA-GRAMMOTOXIN SIA'''<br />
'''SOLUTION STRUCTURE OF OMEGA-GRAMMOTOXIN SIA'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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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].
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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://oca.weizmann.ac.il/oca-bin/ocashort?id=1KOZ OCA].
==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12162963 12162963]
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]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Kim, J.I.]]
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[[Category: Kim, J I.]]
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[[Category: Lee, C.W.]]
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[[Category: Lee, C W.]]
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[[Category: Park, E.J.]]
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[[Category: Park, E J.]]
[[Category: Shimada, I.]]
[[Category: Shimada, I.]]
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[[Category: Swartz, K.J.]]
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[[Category: Swartz, K J.]]
[[Category: Takahashi, H.]]
[[Category: Takahashi, H.]]
[[Category: Takeuchi, K.]]
[[Category: Takeuchi, K.]]
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[[Category: toxin]]
[[Category: toxin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:32:19 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:36:24 2008''

Revision as of 11:36, 21 February 2008


1koz

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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 of sequence from [1]. 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

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