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 Bioljournal_title
Current opinion in structural biologyauthors
Walther TH,Ulrich ASdoi
10.1016/j.sbi.2014.05.003subject
Has Abstractpub_date
2014-08-01 00:00:00pages
63-8eissn
0959-440Xissn
1879-033Xpii
S0959-440X(14)00050-5journal_volume
27pub_type
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