Protein-Protein Interactions in the Membrane: Sequence, Structural, and Biological Motifs

by: David T Moore, Bryan W Berger, William F Degrado

Structure, Vol. 16, No. 7. (9 July 2008), pp. 991-1001.

View FullText article

DOI, ScienceDirect

Reviews [Write a review of this article]

There are no reviews of this article

Find related articles from these CiteULike users

jonsta247, zwang, neils

Find related articles with these CiteULike tags

interaction, membrane, motifs, protein, protein-protein, review, structure, temptemp

Abstract

Summary 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.

@article{citeulike:2983691, abstract = {Summary 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.}, author = {Moore, David T. and Berger, Bryan W. and Degrado, William F. }, citeulike-article-id = {2983691}, doi = {10.1016/j.str.2008.05.007}, journal = {Structure}, keywords = {interaction, protein, structure}, month = {July}, number = {7}, pages = {991--1001}, posted-at = {2008-07-14 02:46:16}, priority = {2}, title = {Protein-Protein Interactions in the Membrane: Sequence, Structural, and Biological Motifs}, url = {http://dx.doi.org/10.1016/j.str.2008.05.007}, volume = {16}, year = {2008} }

RIS record

TY - JOUR ID - citeulike:2983691 L3 - citeulike-article-id:2983691 TI - Protein-Protein Interactions in the Membrane: Sequence, Structural, and Biological Motifs JF - Structure VL - 16 IS - 7 SP - 991 EP - 1001 N2 - Summary 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. KW - interaction KW - protein KW - structure AU - Moore, David AU - Berger, Bryan AU - Degrado, William PY - 2008/07/09/ UR - http://dx.doi.org/10.1016/j.str.2008.05.007 ER -

RIS BibTeX