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

The dimerization motif of the glycophorin A transmembrane segment in membranes: Importance of... 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Protein Science Wiley

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

Protein Science , Volume 7 (4) – Apr 1, 1998

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References (23)

Publisher
Wiley
Copyright
Copyright © 1998 The Protein Society
ISSN
0961-8368
eISSN
1469-896X
DOI
10.1002/pro.5560070423
pmid
9568912
Publisher site
See Article on Publisher Site

Abstract

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.

Journal

Protein ScienceWiley

Published: Apr 1, 1998

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