1qmw

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(New page: 200px<br /><applet load="1qmw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qmw" /> '''SOLUTION STRUCTURE OF ALPHA-CONOTOXIN SI'''<...)
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[[Image:1qmw.jpg|left|200px]]<br /><applet load="1qmw" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1qmw.jpg|left|200px]]<br /><applet load="1qmw" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1qmw" />
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'''SOLUTION STRUCTURE OF ALPHA-CONOTOXIN SI'''<br />
'''SOLUTION STRUCTURE OF ALPHA-CONOTOXIN SI'''<br />
==Overview==
==Overview==
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The nuclear magnetic resonance solution structure of alpha-conotoxin SI, has been determined at pH 4.2. The 36 lowest energy structures show that, alpha-conotoxin SI exists in a single major solution conformation and is, stabilized by six hydrogen bonds. Comparisons are made between the SI, solution structure and the solution and crystal structures of, alpha-conotoxin GI. Surprisingly, a high degree of similarity between the, backbone conformations of the GI crystal and the SI solution structures is, seen in the region of lowest sequence homology, namely residues Gly-8 to, Ser-12. This similarity is more surprising when considering that in SI a, proline replaces the Arg-9 found in GI. The correspondence in conformation, in this region provides the definitive evidence that it is the loss of the, arginine basic charge at residue 9 which determines the differences in, toxicity between GI and SI, rather than any changes in conformation, induced by the cyclic proline residue.
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The nuclear magnetic resonance solution structure of alpha-conotoxin SI has been determined at pH 4.2. The 36 lowest energy structures show that alpha-conotoxin SI exists in a single major solution conformation and is stabilized by six hydrogen bonds. Comparisons are made between the SI solution structure and the solution and crystal structures of alpha-conotoxin GI. Surprisingly, a high degree of similarity between the backbone conformations of the GI crystal and the SI solution structures is seen in the region of lowest sequence homology, namely residues Gly-8 to Ser-12. This similarity is more surprising when considering that in SI a proline replaces the Arg-9 found in GI. The correspondence in conformation in this region provides the definitive evidence that it is the loss of the arginine basic charge at residue 9 which determines the differences in toxicity between GI and SI, rather than any changes in conformation induced by the cyclic proline residue.
==About this Structure==
==About this Structure==
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1QMW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Conus_striatus Conus striatus] 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=1QMW OCA].
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1QMW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Conus_striatus Conus striatus] 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=1QMW OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Barany, G.]]
[[Category: Barany, G.]]
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[[Category: Benie, A.J.]]
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[[Category: Benie, A J.]]
[[Category: Hargittai, B.]]
[[Category: Hargittai, B.]]
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[[Category: Janes, R.W.]]
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[[Category: Janes, R W.]]
[[Category: Whitford, D.]]
[[Category: Whitford, D.]]
[[Category: NH2]]
[[Category: NH2]]
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[[Category: venom]]
[[Category: venom]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:49:00 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:41:29 2008''

Revision as of 12:41, 21 February 2008


1qmw

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SOLUTION STRUCTURE OF ALPHA-CONOTOXIN SI

Overview

The nuclear magnetic resonance solution structure of alpha-conotoxin SI has been determined at pH 4.2. The 36 lowest energy structures show that alpha-conotoxin SI exists in a single major solution conformation and is stabilized by six hydrogen bonds. Comparisons are made between the SI solution structure and the solution and crystal structures of alpha-conotoxin GI. Surprisingly, a high degree of similarity between the backbone conformations of the GI crystal and the SI solution structures is seen in the region of lowest sequence homology, namely residues Gly-8 to Ser-12. This similarity is more surprising when considering that in SI a proline replaces the Arg-9 found in GI. The correspondence in conformation in this region provides the definitive evidence that it is the loss of the arginine basic charge at residue 9 which determines the differences in toxicity between GI and SI, rather than any changes in conformation induced by the cyclic proline residue.

About this Structure

1QMW is a Single protein structure of sequence from Conus striatus with as ligand. Full crystallographic information is available from OCA.

Reference

Solution structure of alpha-conotoxin SI., Benie AJ, Whitford D, Hargittai B, Barany G, Janes RW, FEBS Lett. 2000 Jul 7;476(3):287-95. PMID:10913630

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