A dimerization motif for transmembrane alpha-helices.
Specific helix-helix interactions inside lipid bilayers guide the folding and assembly of many integral membrane proteins and their complexes. We report here a pattern of 7 amino acids (LIxxGVxxGVxxT) which when introduced into several hydrophobic transmembrane alpha-helices promotes their specific dimerization. Dimerization is driven by interactions that are specific, dominated by the helix-helix interface, and involve no potentially ionizable groups. The motif may provide a useful tool for the functional analysis of such interactions in a variety of systems. Further, since this particular motif is rare, whilst specific helix association is not, many other such motifs may exist, which could permit sorting within complex membranes as well as guiding folding and oligomerization.
Lemmon
M A
MA
Department of Molecular Biophysics & Biochemistry, Yale University, New Haven, CT 06520, USA.
Treutlein
H R
HR
Adams
P D
PD
Brünger
A T
AT
Engelman
D M
DM
D000595:Amino Acid Sequence; D000818:Animals; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry* / Q000235:genetics; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017978:Receptors, Growth Factor / Q000737:chemistry / Q000235:genetics
D008565:Membrane Proteins; D010455:Peptides; D017978:Receptors, Growth Factor; C027819:polyleucine