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Structure. 2008 Jul;16(7):991-1001. doi: 10.1016/j.str.2008.05.007.

Protein-protein interactions in the membrane: sequence, structural, and biological motifs.

Author information

1
Department of Biochemistry and Molecular Biophysics, School of Medicine, University of Pennsylvania, Philadelphia, PA 19104-6059, USA.

Abstract

Single-span transmembrane (TM) helices have structural and functional roles well beyond serving as mere anchors to tether water-soluble domains in the vicinity of the membrane. They frequently direct the assembly of protein complexes and mediate signal transduction in ways analogous to small modular domains in water-soluble proteins. This review highlights different sequence and structural motifs that direct TM assembly and discusses their roles in diverse biological processes. We believe that TM interactions are potential therapeutic targets, as evidenced by natural proteins that modulate other TM interactions and recent developments in the design of TM-targeting peptides.

PMID:
18611372
PMCID:
PMC3771515
DOI:
10.1016/j.str.2008.05.007
[Indexed for MEDLINE]
Free PMC Article

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