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


     

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
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 Orzaez, M.
Right arrow Articles by Mingarro, I.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Orzaez, M.
Right arrow Articles by Mingarro, I.
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?

Protein Science, Vol 9, Issue 6 1246-1253, Copyright © 2000 by The Protein Society

Influence of the C-terminus of the glycophorin A transmembrane fragment on the dimerization process [In Process Citation]

M Orzaez, E Perez-Paya and I Mingarro
Departament de Bioquimica i Biologia Molecular, Universitat de Valencia, Burjassot, Spain.

The monomer-dimer equilibrium of the glycophorin A (GpA) transmembrane (TM) fragment has been used as a model system to investigate the amino acid sequence requirements that permit an appropriate helix-helix packing in a membrane-mimetic environment. In particular, we have focused on a region of the helix where no crucial residues for packing have been yet reported. Various deletion and replacement mutants in the C-terminal region of the TM fragment showed that the distance between the dimerization motif and the flanking charged residues from the cytoplasmic side of the protein is important for helix packing. Furthermore, selected GpA mutants have been used to illustrate the rearrangement of TM fragments that takes place when leucine repeats are introduced in such protein segments. We also show that secondary structure of GpA derivatives was independent from dimerization, in agreement with the two-stage model for membrane protein folding and oligomerization.
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
D. Thevenin and T. Lazarova
Stable interactions between the transmembrane domains of the adenosine A2A receptor
Protein Sci., July 1, 2008; 17(7): 1188 - 1199.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
L. E. Fisher, D. M. Engelman, and J. N. Sturgis
Effect of Detergents on the Association of the Glycophorin A Transmembrane Helix
Biophys. J., November 1, 2003; 85(5): 3097 - 3105.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
S. Sharpe, K. R. Barber, C. W. M. Grant, D. Goodyear, and M. R. Morrow
Organization of Model Helical Peptides in Lipid Bilayers: Insight into the Behavior of Single-Span Protein Transmembrane Domains
Biophys. J., July 1, 2002; 83(1): 345 - 358.
[Abstract] [Full Text] [PDF]

Home page
 BloodHome page
I. Auffray, S. Marfatia, K. de Jong, G. Lee, C.-H. Huang, C. Paszty, M. J. A. Tanner, N. Mohandas, and J. A. Chasis
Glycophorin A dimerization and band 3 interaction during erythroid membrane biogenesis: in vivo studies in human glycophorin A transgenic mice
Blood, May 1, 2001; 97(9): 2872 - 2878.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2000 by The Protein Society.