Protein Science CSH PROT
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Protein Science (2004), 13:555-559. Published by Cold Spring Harbor Laboratory Press. Copyright © 2004 The Protein Society
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Ruan, W.
Right arrow Articles by Langosch, D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ruan, W.
Right arrow Articles by Langosch, D.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

FOR THE RECORD

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

Weiming Ruan, Eric Lindner and Dieter Langosch

Lehrstuhl Chemie der Biopolymere, Technische Universität München, 85354 Freising, Germany

(RECEIVED August 8, 2003; FINAL REVISION October 15, 2003; ACCEPTED October 15, 2003)



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.

Keywords: Membrane protein; asparagine; leucine zipper; protein–protein interaction; transmembrane segment

Reprint requests to: Dieter Langosch, Lehrstuhl für Chemie der Biopolymere, Technische Universität München, Weihenstephaner Berg 3, D-85354 Freising-Weihenstephan, Germany; e-mail: biopolymere{at}bl.tum.de; fax: 49-8161-71-44-04.

Article and publication are at http://www.proteinscience.org/cgi/doi/10.1110/ps.03357404.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 Protein Sci.Home page
K. Parthasarathy, X. Lin, S. M. Tan, S.K. A. Law, and J. Torres
Transmembrane helices that form two opposite homodimeric interactions: An asparagine scan study of {alpha}M and {beta}2 integrins
Protein Sci., May 1, 2008; 17(5): 930 - 938.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
B. D. Wines, H. M. Trist, P. A. Ramsland, and P. M. Hogarth
A Common Site of the Fc Receptor {gamma} Subunit Interacts with the Unrelated Immunoreceptors Fc{alpha}RI and Fc{epsilon}RI
J. Biol. Chem., June 23, 2006; 281(25): 17108 - 17113.
[Abstract] [Full Text] [PDF]

Home page
 Protein Sci.Home page
K. P. Howard, W. Liu, E. Crocker, V. Nanda, J. Lear, W. F. Degrado, and S. O. Smith
Rotational orientation of monomers within a designed homo-oligomer transmembrane helical bundle
Protein Sci., April 1, 2005; 14(4): 1019 - 1024.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2004 by The Protein Society.