The cystine‐stabilized α‐helix: A common structural motif of ion‐channel blocking neurotoxic peptides | Zendy

Kobayashi Yuji | Zendy; Takashima Hiroyuki | Zendy; Tamaoki Haruhiko | Zendy; Kyogoku Yoshimasa | Zendy; Lambert Paul | Zendy; Kuroda Hisaya | Zendy; Chino Naoyoshi | Zendy; Watanabe Takushi X. | Zendy; Kimura Terutoshi | Zendy; Sakakibara Shumpei | Zendy; Moroder Luis | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Premium

The cystine‐stabilized α‐helix: A common structural motif of ion‐channel blocking neurotoxic peptides

Author(s) -

Kobayashi Yuji,

Takashima Hiroyuki,

Tamaoki Haruhiko,

Kyogoku Yoshimasa,

Lambert Paul,

Kuroda Hisaya,

Chino Naoyoshi,

Watanabe Takushi X.,

Kimura Terutoshi,

Sakakibara Shumpei,

Moroder Luis

Publication year - 1991

Publication title -

biopolymers

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.556

H-Index - 125

eISSN - 1097-0282

pISSN - 0006-3525

DOI - 10.1002/bip.360311009

Subject(s) - chemistry , charybdotoxin , cystine , structural motif , stereochemistry , ion channel , crystallography , biophysics , cysteine , biochemistry , enzyme , receptor , biology , membrane potential

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.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here

Accelerating Research