Transmembrane helix dimerization: Beyond the search for sequence motifs

Edwin Li, William C. Wimley, Kalina Hristova

Research output: Contribution to journalReview article

Abstract

Studies of the dimerization of transmembrane (TM) helices have been ongoing for many years now, and have provided clues to the fundamental principles behind membrane protein (MP) folding. Our understanding of TM helix dimerization has been dominated by the idea that sequence motifs, simple recognizable amino acid sequences that drive lateral interaction, can be used to explain and predict the lateral interactions between TM helices in membrane proteins. But as more and more unique interacting helices are characterized, it is becoming clear that the sequence motif paradigm is incomplete. Experimental evidence suggests that the search for sequence motifs, as mediators of TM helix dimerization, cannot solve the membrane protein folding problem alone. Here we review the current understanding in the field, as it has evolved from the paradigm of sequence motifs into a view in which the interactions between TM helices are much more complex. This article is part of a Special Issue entitled: Membrane protein structure and function.

Original languageEnglish (US)
Pages (from-to)183-193
Number of pages11
JournalBiochimica et Biophysica Acta - Biomembranes
Volume1818
Issue number2
DOIs
StatePublished - Feb 1 2012

Keywords

  • Membrane protein folding
  • Sequence motif
  • Transmembrane helix dimerization

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Cell Biology

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