A transmembrane helix dimer: structure and implications.
The three-dimensional structure of the dimeric transmembrane domain of glycophorin A (GpA) was determined by solution nuclear magnetic resonance spectroscopy of a 40-residue peptide solubilized in aqueous detergent micelles. The GpA membrane-spanning alpha helices cross at an angle of -40 degrees and form a small but well-packed interface that lacks intermonomer hydrogen bonds. The structure provides an explanation for the previously characterized sequence dependence of GpA dimerization and demonstrates that van der Waals interactions alone can mediate stable and specific associations between transmembrane helices.
MacKenzie
K R
KR
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8114, USA.
Prestegard
J H
JH
Engelman
D M
DM
D000595:Amino Acid Sequence; D019281:Dimerization; D004910:Erythrocyte Membrane / Q000737:chemistry*; D005998:Glycine / Q000737:chemistry; D006021:Glycophorins / Q000737:chemistry*; D006860:Hydrogen Bonding; D009682:Magnetic Resonance Spectroscopy; D008823:Micelles; D008958:Models, Molecular; D008969:Molecular Sequence Data; D016296:Mutagenesis; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011993:Recombinant Fusion Proteins / Q000737:chemistry
D006021:Glycophorins; D008823:Micelles; D011993:Recombinant Fusion Proteins; D005998:Glycine