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Protein Sci. 2004 Feb;13(2):555-9.

The interface of a membrane-spanning leucine zipper mapped by asparagine-scanning mutagenesis.

Author information

1
Lehrstuhl für Chemie der Biopolymere, Technische Universität München, Weihenstephaner Berg 3, D-85354 Freising-Weihenstephan, Germany.

Abstract

An oligo-leucine sequence has previously been shown to function as an artificial transmembrane segment that efficiently self-assembles in membranes and in detergent solution. Here, a novel technique, asparagine-scanning mutagenesis, was applied to probe the interface of the self-assembled oligo-leucine domain. This novel approach identifies interfacial residues whose exchange to asparagine leads to enhanced self-interaction of transmembrane helices by interhelical hydrogen bond formation. As analyzed by the ToxR system in membranes, the interface formed by the oligo-leucine domain is based on a leucine-zipper-like heptad repeat pattern of amino acids. In general, the strongest impacts on self-assembly were seen with asparagines located around the center of the sequence, indicating that interaction is be more efficient here than at the termini of the transmembrane domains.

PMID:
14739334
PMCID:
PMC2286708
DOI:
10.1110/ps.03357404
[Indexed for MEDLINE]
Free PMC Article

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