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1ul2

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(New page: 200px<br /><applet load="1ul2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ul2" /> '''Solution Conformation of alpha-Conotoxin GIC...)
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[[Image:1ul2.jpg|left|200px]]<br /><applet load="1ul2" size="350" color="white" frame="true" align="right" spinBox="true"
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'''Solution Conformation of alpha-Conotoxin GIC'''<br />
'''Solution Conformation of alpha-Conotoxin GIC'''<br />
==Overview==
==Overview==
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Alpha-conotoxin GIC is a 16-residue peptide isolated from the venom of the, cone snail Conus geographus. Alpha-conotoxin GIC potently blocks the, alpha3beta2 subtype of human nicotinic acetylcholine receptor, showing a, high selectivity for neuronal versus muscle subtype [McIntosh, Dowell, Watkins, Garrett, Yoshikami, and Olivera (2002) J. Biol. Chem. 277, 33610-33615]. We have now determined the three-dimensional solution, structure of alpha-conotoxin GIC by NMR spectroscopy. The structure of, alpha-conotoxin GIC is well defined with backbone and heavy atom root mean, square deviations (residues 2-16) of 0.53 A and 0.96 A respectively., Structure and surface comparison of alpha-conotoxin GIC with the other, alpha4/7 subfamily conotoxins reveals unique structural aspects of, alpha-conotoxin GIC. In particular, the structural comparison between, alpha-conotoxins GIC and MII indicates molecular features that may confer, their similar receptor specificity profile, as well as those that provide, the unique binding characteristics of alpha-conotoxin GIC.
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Alpha-conotoxin GIC is a 16-residue peptide isolated from the venom of the cone snail Conus geographus. Alpha-conotoxin GIC potently blocks the alpha3beta2 subtype of human nicotinic acetylcholine receptor, showing a high selectivity for neuronal versus muscle subtype [McIntosh, Dowell, Watkins, Garrett, Yoshikami, and Olivera (2002) J. Biol. Chem. 277, 33610-33615]. We have now determined the three-dimensional solution structure of alpha-conotoxin GIC by NMR spectroscopy. The structure of alpha-conotoxin GIC is well defined with backbone and heavy atom root mean square deviations (residues 2-16) of 0.53 A and 0.96 A respectively. Structure and surface comparison of alpha-conotoxin GIC with the other alpha4/7 subfamily conotoxins reveals unique structural aspects of alpha-conotoxin GIC. In particular, the structural comparison between alpha-conotoxins GIC and MII indicates molecular features that may confer their similar receptor specificity profile, as well as those that provide the unique binding characteristics of alpha-conotoxin GIC.
==About this Structure==
==About this Structure==
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1UL2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with NH2 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UL2 OCA].
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1UL2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=NH2:'>NH2</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UL2 OCA].
==Reference==
==Reference==
Solution conformation of alpha-conotoxin GIC, a novel potent antagonist of alpha3beta2 nicotinic acetylcholine receptors., Chi SW, Kim DH, Olivera BM, McIntosh JM, Han KH, Biochem J. 2004 Jun 1;380(Pt 2):347-52. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14992691 14992691]
Solution conformation of alpha-conotoxin GIC, a novel potent antagonist of alpha3beta2 nicotinic acetylcholine receptors., Chi SW, Kim DH, Olivera BM, McIntosh JM, Han KH, Biochem J. 2004 Jun 1;380(Pt 2):347-52. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14992691 14992691]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Chi, S.W.]]
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[[Category: Chi, S W.]]
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[[Category: Han, K.H.]]
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[[Category: Han, K H.]]
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[[Category: Kim, D.H.]]
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[[Category: Kim, D H.]]
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[[Category: McIntosh, J.M.]]
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[[Category: McIntosh, J M.]]
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[[Category: Olivera, B.M.]]
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[[Category: Olivera, B M.]]
[[Category: NH2]]
[[Category: NH2]]
[[Category: alpha-helix]]
[[Category: alpha-helix]]
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[[Category: two disulfide bonds]]
[[Category: two disulfide bonds]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 04:12:45 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:25:42 2008''

Revision as of 13:25, 21 February 2008


1ul2

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Solution Conformation of alpha-Conotoxin GIC

Overview

Alpha-conotoxin GIC is a 16-residue peptide isolated from the venom of the cone snail Conus geographus. Alpha-conotoxin GIC potently blocks the alpha3beta2 subtype of human nicotinic acetylcholine receptor, showing a high selectivity for neuronal versus muscle subtype [McIntosh, Dowell, Watkins, Garrett, Yoshikami, and Olivera (2002) J. Biol. Chem. 277, 33610-33615]. We have now determined the three-dimensional solution structure of alpha-conotoxin GIC by NMR spectroscopy. The structure of alpha-conotoxin GIC is well defined with backbone and heavy atom root mean square deviations (residues 2-16) of 0.53 A and 0.96 A respectively. Structure and surface comparison of alpha-conotoxin GIC with the other alpha4/7 subfamily conotoxins reveals unique structural aspects of alpha-conotoxin GIC. In particular, the structural comparison between alpha-conotoxins GIC and MII indicates molecular features that may confer their similar receptor specificity profile, as well as those that provide the unique binding characteristics of alpha-conotoxin GIC.

About this Structure

1UL2 is a Single protein structure of sequence from [1] with as ligand. Full crystallographic information is available from OCA.

Reference

Solution conformation of alpha-conotoxin GIC, a novel potent antagonist of alpha3beta2 nicotinic acetylcholine receptors., Chi SW, Kim DH, Olivera BM, McIntosh JM, Han KH, Biochem J. 2004 Jun 1;380(Pt 2):347-52. PMID:14992691

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