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Tryptophan supports interaction of transmembrane helices.

Abstract：

:Interactions of transmembrane helices play an important role in folding and oligomerization of integral membrane proteins. The interfacial residues of these helices frequently correspond to heptad repeat motifs. In order to uncover novel mechanisms underlying these interactions, we randomised a heptad repeat pattern with a complete set of amino acids. Those sequences that were capable of high-affinity self-interaction upon integration into bacterial inner membranes were selected by means of the POSSYCCAT system. A comparison between selected and non-selected sequences reveals that high-affinity sequences were strongly enriched in tryptophan residues that accumulated at specific positions of the heptad motif. Mutation of Trp in selected clones significantly reduced self-interaction of the transmembrane segments without affecting their efficiency of membrane integration. Conversely, grafting Trp onto artificial transmembrane segments strongly enhanced their interaction. We conclude that tryptophan supports interaction of transmembrane segments.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Ridder A,Skupjen P,Unterreitmeier S,Langosch D

doi

10.1016/j.jmb.2005.09.084

keywords:

subject

Has Abstract

pub_date

2005-12-09 00:00:00

pages

894-902

issue

4

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(05)01163-0

journal_volume

354

pub_type

杂志文章

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