THE CYSTINE-STABILIZED ALPHA-HELIX - A COMMON STRUCTURAL MOTIF OF ION-CHANNEL BLOCKING NEUROTOXIC PEPTIDES

被引：99

作者：

KOBAYASHI, Y

TAKASHIMA, H

TAMAOKI, H

KYOGOKU, Y

LAMBERT, P

KURODA, H

CHINO, N

WATANABE, TX

KIMURA, T

SAKAKIBARA, S

MORODER, L

机构：

[1] KURARAY CO LTD,RES LABS,KURASHIKI,OKAYAMA 710,JAPAN

[2] PEPTIDE INST INC,PROT RES FDN,MINO,OSAKA 562,JAPAN

[3] MAX PLANCK INST BIOCHEM,W-8033 MARTINSRIED,GERMANY

来源：

BIOPOLYMERS | 1991年 / 31卷 / 10期

关键词：

D O I：

10.1002/bip.360311009

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

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页码：1213 / 1220

页数：8

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