1eyo

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(New page: 200px<br /><applet load="1eyo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1eyo" /> '''SOLUTION STRUCTURE OF CONOTOXIN TVIIA FROM C...)
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'''SOLUTION STRUCTURE OF CONOTOXIN TVIIA FROM CONUS TULIPA'''<br />
'''SOLUTION STRUCTURE OF CONOTOXIN TVIIA FROM CONUS TULIPA'''<br />
==Overview==
==Overview==
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The three-dimensional solution structure of conotoxin TVIIA, a 30-residue, polypeptide from the venom of the piscivorous cone snail Conus tulipa, has, been determined using 2D 1H NMR spectroscopy. TVIIA contains six cysteine, residues which form a 'four-loop' structural framework common to many, peptides from Conus venoms including the omega-, delta-, kappa-, and, muO-conotoxins. However, TVIIA does not belong to these well-characterized, pharmacological classes of conotoxins, but displays high sequence identity, with conotoxin GS, a muscle sodium channel blocker from Conus geographus., Structure calculations were based on 562 interproton distance restraints, inferred from NOE data, together with 18 backbone and nine side-chain, torsion angle restraints derived from spin-spin coupling constants. The, final family of 20 structures had mean pairwise rms differences over, residues 2-27 of 0.18+/-0.05 A for the backbone atoms and 1.39+/-0.33 A, for all heavy atoms. The structure consists of a triple-stranded, antiparallel beta sheet with +2x, -1 topology (residues 7-9, 16-20 and, 23-27) and several beta turns. The core of the molecule is formed by three, disulfide bonds which form a cystine knot motif common to many toxic and, inhibitory polypeptides. The global fold, molecular shape and distribution, of amino-acid sidechains in TVIIA is similar to that previously reported, for conotoxin GS, and comparison with other four-loop conotoxin structures, provides further indication that TVIIA and GS represent a new and distinct, subgroup of this structural family. The structure of TVIIA determined in, this study provides the basis for determining a structure-activity, relationship for these molecules and their interaction with target, receptors.
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The three-dimensional solution structure of conotoxin TVIIA, a 30-residue polypeptide from the venom of the piscivorous cone snail Conus tulipa, has been determined using 2D 1H NMR spectroscopy. TVIIA contains six cysteine residues which form a 'four-loop' structural framework common to many peptides from Conus venoms including the omega-, delta-, kappa-, and muO-conotoxins. However, TVIIA does not belong to these well-characterized pharmacological classes of conotoxins, but displays high sequence identity with conotoxin GS, a muscle sodium channel blocker from Conus geographus. Structure calculations were based on 562 interproton distance restraints inferred from NOE data, together with 18 backbone and nine side-chain torsion angle restraints derived from spin-spin coupling constants. The final family of 20 structures had mean pairwise rms differences over residues 2-27 of 0.18+/-0.05 A for the backbone atoms and 1.39+/-0.33 A for all heavy atoms. The structure consists of a triple-stranded, antiparallel beta sheet with +2x, -1 topology (residues 7-9, 16-20 and 23-27) and several beta turns. The core of the molecule is formed by three disulfide bonds which form a cystine knot motif common to many toxic and inhibitory polypeptides. The global fold, molecular shape and distribution of amino-acid sidechains in TVIIA is similar to that previously reported for conotoxin GS, and comparison with other four-loop conotoxin structures provides further indication that TVIIA and GS represent a new and distinct subgroup of this structural family. The structure of TVIIA determined in this study provides the basis for determining a structure-activity relationship for these molecules and their interaction with target receptors.
==About this Structure==
==About this Structure==
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1EYO 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=1EYO OCA].
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1EYO 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=1EYO OCA].
==Reference==
==Reference==
Conotoxin TVIIA, a novel peptide from the venom of Conus tulipa 2. Three-dimensional solution structure., Hill JM, Alewood PF, Craik DJ, Eur J Biochem. 2000 Aug;267(15):4649-57. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10903497 10903497]
Conotoxin TVIIA, a novel peptide from the venom of Conus tulipa 2. Three-dimensional solution structure., Hill JM, Alewood PF, Craik DJ, Eur J Biochem. 2000 Aug;267(15):4649-57. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10903497 10903497]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Alewood, P.F.]]
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[[Category: Alewood, P F.]]
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[[Category: Craik, D.J.]]
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[[Category: Craik, D J.]]
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[[Category: Hill, J.M.]]
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[[Category: Hill, J M.]]
[[Category: cystine knot motif]]
[[Category: cystine knot motif]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:33:16 2008''

Revision as of 10:33, 21 February 2008


1eyo

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SOLUTION STRUCTURE OF CONOTOXIN TVIIA FROM CONUS TULIPA

Overview

The three-dimensional solution structure of conotoxin TVIIA, a 30-residue polypeptide from the venom of the piscivorous cone snail Conus tulipa, has been determined using 2D 1H NMR spectroscopy. TVIIA contains six cysteine residues which form a 'four-loop' structural framework common to many peptides from Conus venoms including the omega-, delta-, kappa-, and muO-conotoxins. However, TVIIA does not belong to these well-characterized pharmacological classes of conotoxins, but displays high sequence identity with conotoxin GS, a muscle sodium channel blocker from Conus geographus. Structure calculations were based on 562 interproton distance restraints inferred from NOE data, together with 18 backbone and nine side-chain torsion angle restraints derived from spin-spin coupling constants. The final family of 20 structures had mean pairwise rms differences over residues 2-27 of 0.18+/-0.05 A for the backbone atoms and 1.39+/-0.33 A for all heavy atoms. The structure consists of a triple-stranded, antiparallel beta sheet with +2x, -1 topology (residues 7-9, 16-20 and 23-27) and several beta turns. The core of the molecule is formed by three disulfide bonds which form a cystine knot motif common to many toxic and inhibitory polypeptides. The global fold, molecular shape and distribution of amino-acid sidechains in TVIIA is similar to that previously reported for conotoxin GS, and comparison with other four-loop conotoxin structures provides further indication that TVIIA and GS represent a new and distinct subgroup of this structural family. The structure of TVIIA determined in this study provides the basis for determining a structure-activity relationship for these molecules and their interaction with target receptors.

About this Structure

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

Reference

Conotoxin TVIIA, a novel peptide from the venom of Conus tulipa 2. Three-dimensional solution structure., Hill JM, Alewood PF, Craik DJ, Eur J Biochem. 2000 Aug;267(15):4649-57. PMID:10903497

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