A dimerization motif for transmembrane α–helices
作者： Mark A. Lemmon , Herbert R. Treutlein , Paul D. Adams , Axel T. Brünger , Donald M. Engelman
DOI: 10.1038/NSB0394-157
关键词: Peptide sequence 、 Protein structure 、 Protein folding 、 Crystallography 、 Integral membrane protein 、 Amino acid 、 Membrane 、 Lipid bilayer 、 Biophysics 、 Chemistry 、 Transmembrane protein
摘要: Specific helix-helix interactions inside lipid bilayers guide the folding and assembly of many integral membrane proteins their complexes. We report here a pattern 7 amino acids (LIxxGVxxGVxxT) which when introduced into several hydrophobic transmembrane alpha-helices promotes specific dimerization. Dimerization is driven by that are specific, dominated interface, involve no potentially ionizable groups. The motif may provide useful tool for functional analysis such in variety systems. Further, since this particular rare, whilst helix association not, other motifs exist, could permit sorting within complex membranes as well guiding oligomerization.
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