Access the full text.
Sign up today, get DeepDyve free for 14 days.
Gregg Dieckmann, W. DeGrado (1997)
Modeling transmembrane helical oligomers.Current opinion in structural biology, 7 4
M. Lemmon, H. Treutlein, P. Adams, A. Brünger, D. Engelman (1994)
A dimerization motif for transmembrane α–helicesNature Structural Biology, 1
(1996)
A peptide derived from a beta2-adrenergic receptor transmembrane
D. Langosch, Bettina Brosig, H. Kolmar, H. Fritz (1996)
Dimerisation of the glycophorin A transmembrane segment in membranes probed with the ToxR transcription activator.Journal of molecular biology, 263 4
H. Kolmar, C. Frisch, G. Kleemann, K. Götze, F. Stevens, H. Fritz (1994)
Dimerization of Bence Jones proteins: linking the rate of transcription from an Escherichia coli promoter to the association constant of REIV.Biological chemistry Hoppe-Seyler, 375 1
P. Adams, D. Engelman, A. Brünger (1996)
Improved prediction for the structure of the dimeric transmembrane domain of glycophorin A obtained through global searchingProteins: Structure, 26
T. Hébert, S. Moffett, J. Morello, T. Loisel, D. Bichet, C. Barret, M. Bouvier (1996)
A Peptide Derived from a β2-Adrenergic Receptor Transmembrane Domain Inhibits Both Receptor Dimerization and Activation*The Journal of Biological Chemistry, 271
M. Lemmon, D. Engelman (1994)
Specificity and promiscuity in membrane helix interactionsQuarterly Reviews of Biophysics, 27
I. Mingarro, P. Whitley, G. Heijne, M. Lemmon (1996)
Ala‐insertion scanning mutagenesis of the glycophorin a transmembrane helix: A rapid way to map helix‐helix interactions in integral membrane proteinsProtein Science, 5
H. Kolmar, F. Hennecke, K. Götze, B. Janzer, B. Vogt, F. Mayer, H. Fritz (1995)
Membrane insertion of the bacterial signal transduction protein ToxR and requirements of transcription activation studied by modular replacement of different protein substructures.The EMBO Journal, 14
Mark LemmonS, J. Flanagan, J. Hunt, B. Adair, Barbara-Jean Bormanng, Christopher Dempseyll, D. Engelman (1992)
Glycophorin A dimerization is driven by specific interactions between transmembrane alpha-helices.The Journal of biological chemistry, 267 11
Huan Chen, D. Kendall (1995)
Artificial Transmembrane Segments.The Journal of Biological Chemistry, 270
Engelman DM. 1997. A transmembrane helix 163
Kunkel (1987)
Rapid and efficient site-specific mutagenesis without phenotypic selectionMethods Enzymol, 154
M. Lemmon, Herbert Treutlein, Paul Adams, A. Brunger, Donald Engelman (1994)
A dimerization motif for transmembrane alpha-helices.Nature structural biology, 1 3
V. Asundi, D. Carey (1995)
Self-association of N-Syndecan (Syndecan-3) Core Protein Is Mediated by a Novel Structural Motif in the Transmembrane Domain and Ectodomain Flanking Region (*)The Journal of Biological Chemistry, 270
K. Williams, M. Glibowicka, Zuomei Li, Hong Li, Amir Khan, Yv Chen, Jing Wang, D. Marvin, C. Deber (1995)
Packing of coat protein amphipathic and transmembrane helices in filamentous bacteriophage M13: role of small residues in protein oligomerization.Journal of molecular biology, 252 1
M. Lemmon, John Flanagan, Herbert Treutlein, Jian Zhang, D. Engelman (1992)
Sequence specificity in the dimerization of transmembrane alpha-helices.Biochemistry, 31 51
V. DiRita (1992)
Co‐ordinate expression of virulence genes by ToxR in Vibrio choleraeMolecular Microbiology, 6
H. Bedouelle, P. Duplay (1988)
Production in Escherichia coli and one-step purification of bifunctional hybrid proteins which bind maltose. Export of the Klenow polymerase into the periplasmic space.European journal of biochemistry, 171 3
P. Cosson, J. Bonifacino (1992)
Role of transmembrane domain interactions in the assembly of class II MHC molecules.Science, 258 5082
T. Kunkel, J. Roberts, R. Zakour (1987)
Rapid and efficient site-specific mutagenesis without phenotypic selection.Methods in enzymology, 154
K. MacKenzie, J. Prestegard, D. Engelman (1997)
A Transmembrane Helix Dimer: Structure and Implications, 276
The glycophorin A transmembrane segment homodimerizes to a right‐handed pair of α‐helices. Here, we identified the amino acid motif mediating this interaction within a natural membrane environment. Critical residues were grafted onto two different hydrophobic host sequences in a stepwise manner and self‐assembly of the hybrid sequences was determined with the ToxR transcription activator system. Our results show that the motif LIxxGxxxGxxxT elicits a level of self‐association equivalent to that of the original glycophorin A transmembrane segment. This motif is very similar to the one previously established in detergent solution. Interestingly, the central GxxxG motif by itself already induced strong self‐assembly of host sequences and the three‐residue spacing between both glycines proved to be optimal for the interaction. The GxxxG element thus appears to be the most crucial part of the interaction motif.
Protein Science – Wiley
Published: Apr 1, 1998
Read and print from thousands of top scholarly journals.
Already have an account? Log in
Bookmark this article. You can see your Bookmarks on your DeepDyve Library.
To save an article, log in first, or sign up for a DeepDyve account if you don’t already have one.
Copy and paste the desired citation format or use the link below to download a file formatted for EndNote
Access the full text.
Sign up today, get DeepDyve free for 14 days.
All DeepDyve websites use cookies to improve your online experience. They were placed on your computer when you launched this website. You can change your cookie settings through your browser.