A DIMERIZATION MOTIF FOR TRANSMEMBRANE ALPHA-HELICES

被引：300
作者：
LEMMON, MA
TREUTLEIN, HR
ADAMS, PD
BRUNGER, AT
ENGELMAN, DM
机构：
[1] YALE UNIV,DEPT MOLEC BIOPHYS & BIOCHEM,NEW HAVEN,CT 06520
[2] YALE UNIV,HOWARD HUGHES MED INST,NEW HAVEN,CT 06520
来源：
NATURE STRUCTURAL BIOLOGY | 1994年 / 1卷 / 03期
关键词：
D O I：
10.1038/nsb0394-157
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：
Specific helix-helix interactions inside lipid bilayers guide the folding and assembly of many integral membrane proteins and their complexes. We report here a pattern of 7 amino acids (LIxxCVxxGVxxT) which when introduced into several hydrophobic transmembrane alpha-helices promotes their specific dimerization. Dimerization is driven by interactions that are specific, dominated by the helix-helix interface, and involve no potentially ionizabIe groups. The motif may provide a useful tool for the functional analysis of such interactions in a variety of systems. Further, since this particular motif is rare, whilst specific helix association is not, many other such motifs may exist, which could permit sorting within complex membranes as well as guiding folding and oligomerization.
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页码：157 / 163
页数：7
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