Transmembrane helix assembly and the role of salt bridges.

Abstract:

:Transmembrane helix-helix interactions mediate the folding and assembly of membrane proteins. Recognition motifs range from GxxxG and leucine zippers to polar side chains and salt bridges. Some canonical membrane proteins contain local charge clusters that are important for folding and function, and which have to be compatible with a stable insertion into the bilayer via the translocon. Recently, the electrostatic "charge zipper" has been described as another kind of assembly motif. The protein sequences exhibit a quasi-symmetrical pattern of complementary charges that can form extended ladders of salt bridges. Such segments can insert reversibly into membranes, or even translocate across them. Nature uses charge zippers in transport processes, and they can also be adapted in the design of cell-penetrating carriers.

journal_name

Curr Opin Struct Biol

authors

Walther TH,Ulrich AS

doi

10.1016/j.sbi.2014.05.003

subject

Has Abstract

pub_date

2014-08-01 00:00:00

pages

63-8

eissn

0959-440X

issn

1879-033X

pii

S0959-440X(14)00050-5

journal_volume

27

pub_type

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