CRYSTAL-STRUCTURE OF DEFENSIN HNP-3, AN AMPHIPHILIC DIMER - MECHANISMS OF MEMBRANE PERMEABILIZATION

被引：444
作者：
HILL, CP
YEE, J
SELSTED, ME
EISENBERG, D
机构：
[1] UNIV CALIF LOS ANGELES,DEPT BIOCHEM,LOS ANGELES,CA 90024
[2] UNIV CALIF LOS ANGELES,DEPT PATHOL,LOS ANGELES,CA 90024
[3] UNIV CALIF LOS ANGELES,DEPT CHEM,LOS ANGELES,CA 90024
[4] UNIV CALIF LOS ANGELES,DEPT MED,LOS ANGELES,CA 90024
来源：
SCIENCE | 1991年 / 251卷 / 5000期
关键词：
D O I：
10.1126/science.2006422
中图分类号：
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
Defensins (molecular weight 3500 to 4000) act in the mammalian immune response by permeabilizing the plasma membranes of a broad spectrum of target organisms, including bacteria, fungi, and enveloped viruses. The high-resolution crystal structure of defensin HNP-3 (1.9 angstrom resolution, R factor 0.19) reveals a dimeric beta-sheet that has an architecture very different from other lytic peptides. The dimeric assembly suggests mechanisms by which defensins might bind to and permeabilize the lipid bilayer.
引用
收藏
页码：1481 / 1485
页数：5
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