A transmembrane helix dimer: structure and implications

KR MacKenzie, JH Prestegard, DM Engelman - Science, 1997 - science.org
Science, 1997science.org
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
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 …
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 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.
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