Abstract:
: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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Benie AJ,Whitford D,Hargittai B,Barany G,Janes RWdoi
10.1016/s0014-5793(00)01724-5keywords:
subject
Has Abstractpub_date
2000-07-07 00:00:00pages
287-95issue
3eissn
0014-5793issn
1873-3468pii
S0014-5793(00)01724-5journal_volume
476pub_type
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