alpha-Helical protein assembly motifs

被引:163
作者
Kohn, WD
Mant, CT
Hodges, RS
机构
[1] UNIV ALBERTA, DEPT BIOCHEM, MRC, GRP PROT STRUCT & FUNCT, EDMONTON, AB T6G 2H7, CANADA
[2] UNIV ALBERTA, PROT ENGN NETWORK CTR EXCELLENCE, EDMONTON, AB T6G 2H7, CANADA
关键词
D O I
10.1074/jbc.272.5.2583
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
This review will focus on alpha-helical protein assembly motifs where the alpha-helix is the major element of secondary structure involved in the folding and stability of the structure and may also be involved in function by binding to receptor molecules. Apart from the three types of alpha-helical motifs discussed, i.e. those motifs that form autonomously folded protein domains; those motifs that only form a stable folded domain when dimerized; and a motif that requires other structural elements to contribute to the hydrophobic core to stabilize a folded domain, we will present examples of more complex protein assemblies that have combined two different motifs to form a functional molecule.
引用
收藏
页码:2583 / 2586
页数:4
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