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. 1998 Apr;7(4):1052–1056. doi: 10.1002/pro.5560070423

The dimerization motif of the glycophorin A transmembrane segment in membranes: importance of glycine residues.

B Brosig 1, D Langosch 1
PMCID: PMC2143994  PMID: 9568912

Abstract

The glycophorin A transmembrane segment homo-dimerizes to a right-handed pair of alpha-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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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