TY - JOUR
T1 - Transmembrane helix dimerization
T2 - Beyond the search for sequence motifs
AU - Li, Edwin
AU - Wimley, William C.
AU - Hristova, Kalina
N1 - Funding Information:
This work was funded by NIH grants GM060000 (WCW), GM068619 (KH) and GM095930 (KH).
PY - 2012/2
Y1 - 2012/2
N2 - Studies of the dimerization of transmembrane (TM) helices have been ongoing for many years now, and have provided clues to the fundamental principles behind membrane protein (MP) folding. Our understanding of TM helix dimerization has been dominated by the idea that sequence motifs, simple recognizable amino acid sequences that drive lateral interaction, can be used to explain and predict the lateral interactions between TM helices in membrane proteins. But as more and more unique interacting helices are characterized, it is becoming clear that the sequence motif paradigm is incomplete. Experimental evidence suggests that the search for sequence motifs, as mediators of TM helix dimerization, cannot solve the membrane protein folding problem alone. Here we review the current understanding in the field, as it has evolved from the paradigm of sequence motifs into a view in which the interactions between TM helices are much more complex. This article is part of a Special Issue entitled: Membrane protein structure and function.
AB - Studies of the dimerization of transmembrane (TM) helices have been ongoing for many years now, and have provided clues to the fundamental principles behind membrane protein (MP) folding. Our understanding of TM helix dimerization has been dominated by the idea that sequence motifs, simple recognizable amino acid sequences that drive lateral interaction, can be used to explain and predict the lateral interactions between TM helices in membrane proteins. But as more and more unique interacting helices are characterized, it is becoming clear that the sequence motif paradigm is incomplete. Experimental evidence suggests that the search for sequence motifs, as mediators of TM helix dimerization, cannot solve the membrane protein folding problem alone. Here we review the current understanding in the field, as it has evolved from the paradigm of sequence motifs into a view in which the interactions between TM helices are much more complex. This article is part of a Special Issue entitled: Membrane protein structure and function.
KW - Membrane protein folding
KW - Sequence motif
KW - Transmembrane helix dimerization
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U2 - 10.1016/j.bbamem.2011.08.031
DO - 10.1016/j.bbamem.2011.08.031
M3 - Review article
C2 - 21910966
AN - SCOPUS:84855465724
SN - 0005-2736
VL - 1818
SP - 183
EP - 193
JO - Biochimica et Biophysica Acta - Biomembranes
JF - Biochimica et Biophysica Acta - Biomembranes
IS - 2
ER -