1d1h
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(New page: 200px<br /><applet load="1d1h" size="450" color="white" frame="true" align="right" spinBox="true" caption="1d1h" /> '''SOLUTION STRUCTURE OF HANATOXIN 1'''<br /> ...)
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Revision as of 10:48, 20 November 2007
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SOLUTION STRUCTURE OF HANATOXIN 1
Overview
The three-dimensional structure of hanatoxin1 (HaTx1) was determined by, using NMR spectroscopy. HaTx1 is a 35 amino acid residue peptide toxin, that inhibits the drk1 voltage-gated K(+) channel not by blocking the, pore, but by altering the energetics of gating. Both the amino acid, sequence of HaTx1 and its unique mechanism of action distinguish this, toxin from the previously described K(+) channel inhibitors. Unlike most, other K(+) channel-blocking toxins, HaTx1 adopts an "inhibitor cystine, knot" motif and is composed of two beta-strands, strand I for residues, 19-21 and strand II for residues 28-30, connected by four chain reversals., A comparison of the surface features of HaTx1 with those of other gating, modifier toxins of voltage-gated Ca(2+) and Na(+) channels suggests that, the combination of a hydrophobic patch and surrounding charged residues is, principally responsible for the binding of gating modifier toxins to, voltage-gated ion channels.
About this Structure
1D1H is a Single protein structure of sequence from Grammostola rosea. Full crystallographic information is available from OCA.
Reference
Solution structure of hanatoxin1, a gating modifier of voltage-dependent K(+) channels: common surface features of gating modifier toxins., Takahashi H, Kim JI, Min HJ, Sato K, Swartz KJ, Shimada I, J Mol Biol. 2000 Mar 31;297(3):771-80. PMID:10731427
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