Membrane protein folding: beyond the two stage model.
The folding of alpha-helical membrane proteins has previously been described using the two stage model, in which the membrane insertion of independently stable alpha-helices is followed by their mutual interactions within the membrane to give higher order folding and oligomerization. Given recent advances in our understanding of membrane protein structure it has become apparent that in some cases the model may not fully represent the folding process. Here we present a three stage model which gives considerations to ligand binding, folding of extramembranous loops, insertion of peripheral domains and the formation of quaternary structure.
Engelman
Donald M
DM
Department of Molecular Biophysics and Biochemistry, Yale University, P.O. Box 208114, New Haven, CT 06520-8114, USA. donald.engelman@yale.edu
Chen
Yang
Y
Chin
Chen-Ni
CN
Curran
A Rachael
AR
Dixon
Ann M
AM
Dupuy
Allison D
AD
Lee
Albert S
AS
Lehnert
Ursula
U
Matthews
Erin E
EE
Reshetnyak
Yana K
YK
Senes
Alessandro
A
Popot
Jean-Luc
JL
D020346:Aquaporins / Q000737:chemistry; D001426:Bacterial Proteins / Q000737:chemistry; D001436:Bacteriorhodopsins / Q000737:chemistry; D001665:Binding Sites; D029968:Escherichia coli Proteins / Q000737:chemistry; D008024:Ligands; D008051:Lipid Bilayers / Q000737:chemistry; D008565:Membrane Proteins / Q000737:chemistry*; D008958:Models, Molecular; D015221:Potassium Channels / Q000737:chemistry; D017510:Protein Folding; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D013816:Thermodynamics
D020346:Aquaporins; D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D008024:Ligands; D008051:Lipid Bilayers; D008565:Membrane Proteins; D015221:Potassium Channels; C107790:prokaryotic potassium channel; C078043:GlpF protein, E coli; D001436:Bacteriorhodopsins