A NEW ALPHA-HELICAL MOTIF IN MEMBRANE ACTIVE PEPTIDES

被引：38

作者：

KOBAYASHI, Y

SATO, A

TAKASHIMA, H

TAMAOKI, H

NISHIMURA, S

KYOGOKU, Y

IKENAKA, K

KONDO, T

MIKOSHIBA, K

HOJO, H

AIMOTO, S

MORODER, L

机构：

[1] Institute for Protein Research, Osaka University, Suita, Osaka

来源：

NEUROCHEMISTRY INTERNATIONAL | 1991年 / 18卷 / 04期

关键词：

D O I：

10.1016/0197-0186(91)90151-3

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：

A comparative analysis of the primary and secondary structures of the neurotoxins mast cell degranulating peptide apamina and charybdotoxin, and of the hormone endothelin revealed a strikingly homologous structural element consisting of an alpha-helical stretch spanning the sequence portion Cys-X-X-X-Cys and stabilized by disulfide bridging to a second consensus sequence Cys-X-Cys, itself folded in a beta-type structure. This structural motif generates a certain degree of amphiphilicity for the folded molecules which may be correlated with the bioactivities of the neurotoxins at the membrane level. The presence of the identical structural motif in endothelin raises the question of whether it may represent, even for this hormone, the clue for its biological activity.

引用

页码：525 / 534

页数：10

共 30 条

[1] STRUCTURE OF VARIANT-3 SCORPION NEUROTOXIN FROM CENTRUROIDES-SCULPTURATUS EWING, REFINED AT 1.8 A RESOLUTION [J].