The cystine-stabilized α-helix: A common structural motif of ion-channel blocking neurotoxic peptides
✍ Scribed by Yuji Kobayashi; Hiroyuki Takashima; Haruhiko Tamaoki; Yoshimasa Kyogoku; Paul Lambert; Hisaya Kuroda; Naoyoshi Chino; Takushi X. Watanabe; Terutoshi Kimura; Shumpei Sakakibara; Luis Moroder
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1991
- Tongue
- English
- Weight
- 706 KB
- Volume
- 31
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
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 α‐helical (CSH) motif, which may be correlated with their common ion channel blocking activity.