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The dimerization motif of the glycophorin A transmembrane segment in membranes: Importance of glycine residues
Author(s) -
Brosig Bettina,
Langosch Dieter
Publication year - 1998
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560070423
Subject(s) - glycophorin , motif (music) , transmembrane protein , chemistry , structural motif , transmembrane domain , membrane , glycine , biophysics , biochemistry , stereochemistry , biology , amino acid , physics , receptor , acoustics
The glycophorin A transmembrane segment homodimerizes to a right‐handed pair of α‐helices. Here, we identified the amino acid motif mediating this interaction within a natural membrane environment. Critical residues were grafted onto two different hydrophobic host sequences in a stepwise manner and self‐assembly of the hybrid sequences was determined with the ToxR transcription activator system. Our results show that the motif LIxxGxxxGxxxT elicits a level of self‐association equivalent to that of the original glycophorin A transmembrane segment. This motif is very similar to the one previously established in detergent solution. Interestingly, the central GxxxG motif by itself already induced strong self‐assembly of host sequences and the three‐residue spacing between both glycines proved to be optimal for the interaction. The GxxxG element thus appears to be the most crucial part of the interaction motif.