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Influence of the C-terminus of the glycophorin A transmembrane fragment on the dimerization process

Published online by Cambridge University Press:  01 June 2000

MAR ORZÁEZ
Affiliation:
Departament de Bioquímica i Biologia Molecular, Universitat de València, E-46 100 Burjassot, Spain
ENRIQUE PÉREZ-PAYÁ
Affiliation:
Departament de Bioquímica i Biologia Molecular, Universitat de València, E-46 100 Burjassot, Spain
ISMAEL MINGARRO
Affiliation:
Departament de Bioquímica i Biologia Molecular, Universitat de València, E-46 100 Burjassot, Spain
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Abstract

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.

Type
Research Article
Copyright
2000 The Protein Society

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