Solution conformation of conotoxin GI determined by 1H nuclear magnetic resonance spectroscopy and distance geometry calculations

Yuji Kobayashi, Tadayasu Ohkubo, Yoshimasa Kyogoku, Yuji Nishiuchi, Shumpei Sakakibara, Werner Braun, Nobuhiro Go

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Abstract

Conformational analysis of conotoxin GI, one of the neurotoxic peptides produced by a marine snail, genus Conus, was performed by a combination of nuclear magnetic resonance spectroscopy (NMR) and distance geometry calculations. The resulting conformers on minimization of the target function were classified into two groups. The difference in the structures of the conformers is mainly due to the difference in the orientation of the side chain of the tyrosyl residue. The results show that the solution structure of conotoxin GI satisfies the conformational requirements for the biological activity of an antagonist toward nicotinic cholinergic receptors elucidated in a series of studies on alkaloids. The structure is discussed on the basis of the results of comparison of the atomic arrangements of the active sites of snake venom peptides and molecular models based on the results of secondary structure prediction.

Original languageEnglish (US)
Pages (from-to)4853-4860
Number of pages8
JournalBiochemistry
Volume28
Issue number11
StatePublished - 1989
Externally publishedYes

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ASJC Scopus subject areas

  • Biochemistry

Cite this

Kobayashi, Y., Ohkubo, T., Kyogoku, Y., Nishiuchi, Y., Sakakibara, S., Braun, W., & Go, N. (1989). Solution conformation of conotoxin GI determined by 1H nuclear magnetic resonance spectroscopy and distance geometry calculations. Biochemistry, 28(11), 4853-4860.