1fu3

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(New page: 200px<br /><applet load="1fu3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fu3" /> '''THREE-DIMENSIONAL STRUCTURE IN SOLUTION OF T...)
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'''THREE-DIMENSIONAL STRUCTURE IN SOLUTION OF THE SODIUM CHANNEL AGONIST/ANTAGONIST DELTA-CONOTOXIN TXVIA'''<br />
'''THREE-DIMENSIONAL STRUCTURE IN SOLUTION OF THE SODIUM CHANNEL AGONIST/ANTAGONIST DELTA-CONOTOXIN TXVIA'''<br />
==Overview==
==Overview==
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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.
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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.
==About this Structure==
==About this Structure==
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1FU3 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=1FU3 OCA].
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1FU3 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=1FU3 OCA].
==Reference==
==Reference==
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[[Category: triple-stranded]]
[[Category: triple-stranded]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:17:06 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:42:39 2008''

Revision as of 10:42, 21 February 2008


1fu3

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THREE-DIMENSIONAL STRUCTURE IN SOLUTION OF THE SODIUM CHANNEL AGONIST/ANTAGONIST DELTA-CONOTOXIN TXVIA

Overview

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.

About this Structure

1FU3 is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.

Reference

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

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