1eyo: Difference between revisions
New page: left|200px<br /><applet load="1eyo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1eyo" /> '''SOLUTION STRUCTURE OF CONOTOXIN TVIIA FROM C... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1eyo.jpg|left|200px]]<br /><applet load="1eyo" size=" | [[Image:1eyo.jpg|left|200px]]<br /><applet load="1eyo" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1eyo" /> | caption="1eyo" /> | ||
'''SOLUTION STRUCTURE OF CONOTOXIN TVIIA FROM CONUS TULIPA'''<br /> | '''SOLUTION STRUCTURE OF CONOTOXIN TVIIA FROM CONUS TULIPA'''<br /> | ||
==Overview== | ==Overview== | ||
The three-dimensional solution structure of conotoxin TVIIA, a 30-residue | 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== | ||
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:// | 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]] | ||
[[Category: Alewood, P | [[Category: Alewood, P F.]] | ||
[[Category: Craik, D | [[Category: Craik, D J.]] | ||
[[Category: Hill, J | [[Category: Hill, J M.]] | ||
[[Category: cystine knot motif]] | [[Category: cystine knot motif]] | ||
''Page seeded by [http:// | ''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
|
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
Page seeded by OCA on Thu Feb 21 12:33:16 2008
