Sequence motifs, polar interactions and conformational changes in helical membrane proteins

被引：196

作者：

Curran, AR ^{[1
]}

Engelman, DM ^{[1
]}

机构：

[1] Yale Univ, Dept Mol Biophys & Biochem, New Haven, CT 06520 USA

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 2003年 / 13卷 / 04期

基金：

美国国家卫生研究院; 英国惠康基金; 美国国家科学基金会;

关键词：

D O I：

10.1016/S0959-440X(03)00102-7

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：

The alpha helices of transmembrane proteins interact to form higher order structures. These interactions are frequently mediated by packing motifs (such as GxxxG) and polar residues. Recent structural data have revealed that small sidechains are able to both stabilize helical membrane proteins and allow conformational changes in the structure. The strong interactions involving polar sidechains often contribute to protein misfolding or malfunction.

引用

页码：412 / 417

页数：6

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