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 α helices cross at an angle of -40 degrees and fo...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 1997-04, Vol.276 (5309), p.131-133
Main Authors: MacKenzie, Kevin R., Prestegard, James H., Engelman, Donald M.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Analytical, structural and metabolic biochemistry
Atoms
Biochemistry
Biological and medical sciences
Dimerization
Dimers
Erythrocyte Membrane - chemistry
Family structure
Fundamental and applied biological sciences. Psychology
Glycine - chemistry
Glycophorin - chemistry
Glycoproteins
Grade Point Average
Hydrogen Bonding
Hydrogen bonds
Literary Devices
Magnetic resonance imaging
Magnetic Resonance Spectroscopy
Membrane proteins
Micelles
Models, Molecular
Molecular Sequence Data
Monomers
Mutagenesis
Nuclear structure
Oxygen
Peptides
Protein Conformation
Protein Folding
Protein Structure, Secondary
Proteins
Recombinant Fusion Proteins - chemistry
Scientific Concepts
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Summary: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 α 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.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.276.5309.131