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1qmw
From Proteopedia
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| - | [[Image:1qmw.jpg|left|200px]] | + | [[Image:1qmw.jpg|left|200px]] |
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| - | '''SOLUTION STRUCTURE OF ALPHA-CONOTOXIN SI''' | + | {{Structure |
| + | |PDB= 1qmw |SIZE=350|CAPTION= <scene name='initialview01'>1qmw</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''SOLUTION STRUCTURE OF ALPHA-CONOTOXIN SI''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1QMW is a [ | + | 1QMW is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Conus_striatus Conus striatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QMW OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10913630 10913630] |
[[Category: Conus striatus]] | [[Category: Conus striatus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: venom]] | [[Category: venom]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:39:52 2008'' |
Revision as of 11:39, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Thu Mar 20 13:39:52 2008
