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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
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.