The cystine-stabilized alpha-helix: a common structural motif of ion-channel blocking neurotoxic peptides.
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.
Kobayashi
Y
Y
Institute for Protein Research, Osaka University, Japan.
Takashima
H
H
Tamaoki
H
H
Kyogoku
Y
Y
Lambert
P
P
Kuroda
H
H
Chino
N
N
Watanabe
T X
TX
Kimura
T
T
Sakakibara
S
S
D000595:Amino Acid Sequence; D000818:Animals; D018999:Charybdotoxin; D003553:Cystine / Q000737:chemistry*; D007473:Ion Channels / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009498:Neurotoxins / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D012604:Scorpion Venoms / Q000737:chemistry; D012689:Sequence Homology, Nucleic Acid
D007473:Ion Channels; D009498:Neurotoxins; D010455:Peptides; D012604:Scorpion Venoms; D018999:Charybdotoxin; D003553:Cystine