Structural aspects of oligomerization taking place between the transmembrane α-helices of bitopic membrane proteins

被引:50
作者
Arkin, IT [1 ]
机构
[1] Hebrew Univ Jerusalem, Dept Biol Chem, Alexander Silberman Inst Life Sci, IL-91904 Jerusalem, Israel
来源
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES | 2002年 / 1565卷 / 02期
基金
英国生物技术与生命科学研究理事会; 以色列科学基金会; 英国惠康基金;
关键词
oligomerization; alpha-helix; bitopic membrane protein;
D O I
10.1016/S0005-2736(02)00580-1
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
Recent advances in biophysical methods have been able to shed more light on the structures of helical bundles formed by the transmembrane segments of bitopic membrane proteins. In this manuscript, I attempt to review the biological importance and diversity of these interactions, the energetics of bundle formation, motifs capable of inducing oligomerization and methods capable of detecting, solving and predicting the structures of these oligomeric bundles. Finally, the structures of the best characterized instances of transmembrane alpha-helical bundles formed by bitopic membrane proteins are described in detail. (C) 2002 Elsevier Science B.V. All tights reserved.
引用
收藏
页码:347 / 363
页数:17
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