Coiled Coils - A Model System for the 21st Century

被引:154
作者
Lupas, Andrei N. [1 ]
Bassler, Jens [1 ]
机构
[1] Max Planck Inst Dev Biol, Dept Prot Evolut, D-72076 Tubingen, Germany
关键词
VIRAL MEMBRANE-FUSION; ALPHA-HELICAL BARRELS; GCN4; LEUCINE-ZIPPER; AMINO-ACID-SEQUENCE; CRYSTAL-STRUCTURE; INFLUENZA HEMAGGLUTININ; MUREIN-LIPOPROTEIN; ESCHERICHIA-COLI; PROTEIN; PARALLEL;
D O I
10.1016/j.tibs.2016.10.007
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
alpha-Helical coiled coils were described more than 60 years ago as simple, repetitive structures mediating oligomerization and mechanical stability. Over the past 20 years, however, they have emerged as one of the most diverse protein folds in nature, enabling many biological functions beyond mechanical rigidity, such as membrane fusion, signal transduction, and solute transport. Despite this great diversity, their structures can be described by parametric equations, making them uniquely suited for rational protein design. Far from having been exhausted as a source of structural insight and a basis for functional engineering, coiled coils are poised to become even more important for protein science in the coming decades.
引用
收藏
页码:130 / 140
页数:11
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