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

Isaiah T. Arkin

doi:10.1016/S0005-2736(02)00580-1

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

Isaiah T. Arkin^*

^*Corresponding author for this work

Department of Biological Chemistry

Research output: Contribution to journal › Review article › peer-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 language	English
Pages (from-to)	347-363
Number of pages	17
Journal	Biochimica et Biophysica Acta - Biomembranes
Volume	1565
Issue number	2
DOIs	https://doi.org/10.1016/S0005-2736(02)00580-1
State	Published - 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

Access to Document

10.1016/S0005-2736(02)00580-1

Cite this

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

Abstract

Bibliographical note

Keywords

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