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1qmw
From Proteopedia
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'''SOLUTION STRUCTURE OF ALPHA-CONOTOXIN SI''' | '''SOLUTION STRUCTURE OF ALPHA-CONOTOXIN SI''' | ||
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[[Category: Janes, R W.]] | [[Category: Janes, R W.]] | ||
[[Category: Whitford, D.]] | [[Category: Whitford, D.]] | ||
| - | [[Category: | + | [[Category: Conotoxin]] |
| - | [[Category: | + | [[Category: Nicotinic acetylcholine receptor]] |
| - | [[Category: | + | [[Category: Toxin]] |
| - | [[Category: | + | [[Category: Venom]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:27:57 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 03:27, 3 May 2008
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. 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 Page seeded by OCA on Sat May 3 06:27:57 2008
