| Literature DB >> 1724185 |
Y Kobayashi1, H Takashima, H Tamaoki, Y Kyogoku, P Lambert, H Kuroda, N Chino, T X Watanabe, T Kimura, S Sakakibara.
Abstract
Neurotoxic peptides from venoms of scorpions and honey bees exhibit a consensus pattern in the two disulfide bridgings related to the sequence portions Cys-X-Cys and Cys-X-X-X-Cys. A revised three-dimensional structure of charybdotoxin, as determined by two-dimensional nmr spectroscopy, confirms that the consensus cystine dislocation generates in all these toxins a common structural element, i.e., the cystine-stabilized alpha-helical (CSH) motif, which may be correlated with their common ion channel blocking activity.Entities:
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Year: 1991 PMID： 1724185 DOI： 10.1002/bip.360311009
Source DB: PubMed Journal: Biopolymers ISSN： 0006-3525 Impact factor: 2.505