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Solution structure of α‐conotoxin SI
Author(s) -
Benie Andrew J.,
Whitford David,
Hargittai Balazs,
Barany George,
Janes Robert W.
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01724-5
Subject(s) - conotoxin , chemistry , residue (chemistry) , proline , crystal structure , crystallography , hydrogen bond , arginine , stereochemistry , amino acid , molecule , peptide , biochemistry , organic chemistry
The nuclear magnetic resonance solution structure of α‐conotoxin SI has been determined at pH 4.2. The 36 lowest energy structures show that α‐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 α‐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.