Structural aspects of oligomerization taking place between the transmembrane α-helices of bitopic membrane proteins

Isaiah T. Arkin*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

52 Scopus citations

Abstract

Recent advances in biophysical methods have been able to shed more light on the structures of helical bundles formed by the transmembrane segments of bitopic membrane proteins. In this manuscript, I attempt to review the biological importance and diversity of these interactions, the energetics of bundle formation, motifs capable of inducing oligomerization and methods capable of detecting, solving and predicting the structures of these oligomeric bundles. Finally, the structures of the best characterized instances of transmembrane α-helical bundles formed by bitopic membrane proteins are described in detail.

Original languageAmerican English
Pages (from-to)347-363
Number of pages17
JournalBiochimica et Biophysica Acta - Biomembranes
Volume1565
Issue number2
DOIs
StatePublished - 11 Oct 2002

Bibliographical note

Funding Information:
Support is acknowledged from the Wellcome Trust (UK), the Biotechnology and Biological Sciences Research Council (UK) and The Israel Science Foundation (grant no. 784/01-16.1). The author is grateful to Professors Cross, Lemmon and MacKenzie for helpful discussion and communicating results before publication.

Keywords

  • Bitopic membrane protein
  • Oligomerization
  • α-Helix

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