Solution structure of α-conotoxin SI
| Autor: | David Whitford, George Barany, Balazs Hargittai, Robert W. Janes, Andrew J. Benie |
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| Rok vydání: | 2000 |
| Předmět: |
Models
Molecular Conotoxin Circular dichroism Magnetic Resonance Spectroscopy Nicotinic acetylcholine receptor Arginine Protein Conformation Stereochemistry Molecular Sequence Data Biophysics Nicotinic Antagonists Crystal structure Biochemistry Nuclear magnetic resonance Crystal Residue (chemistry) Structural Biology Disulfide linked peptide Genetics Animals Amino Acid Sequence Proline Molecular Biology Hydrogen bond Chemistry Circular Dichroism Cell Biology Hydrogen-Ion Concentration Three-dimensional structure Solutions Thermodynamics Conotoxins |
| Zdroj: | FEBS Letters. 476:287-295 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/s0014-5793(00)01724-5 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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