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Science 4 April 1997:
Vol. 276. no. 5309, pp. 131 - 133
DOI: 10.1126/science.276.5309.131
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Reports

A Transmembrane Helix Dimer: Structure and Implications

Kevin R. MacKenzie, James H. Prestegard, Donald M. Engelman *

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.

K. R. MacKenzie and D. M. Engelman, Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8114, USA.
J. H. Prestegard, Department of Chemistry, Yale University, New Haven, CT 06520-8107, USA.
*   To whom correspondence should be addressed.

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The Transmembrane Domain of the E5 Oncoprotein Contains Functionally Discrete Helical Faces.
A. J. Adduci and R. Schlegel (1999)
J. Biol. Chem. 274, 10249-10258
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A Heptad Motif of Leucine Residues Found in Membrane Proteins Can Drive Self-assembly of Artificial Transmembrane Segments.
R. Gurezka, R. Laage, B. Brosig, and D. Langosch (1999)
J. Biol. Chem. 274, 9265-9270
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Interactions between Vaccinia Virus IEV Membrane Proteins and Their Roles in IEV Assembly and Actin Tail Formation.
S. Röttger, F. Frischknecht, I. Reckmann, G. L. Smith, and M. Way (1999)
J. Virol. 73, 2863-2875
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The specificity of interaction of archaeal transducers with their cognate sensory rhodopsins is determined by their transmembrane helices.
X.-N. Zhang, J. Zhu, and J. L. Spudich (1999)
PNAS 96, 857-862
   Abstract »    Full Text »    PDF »
TOXCAT: A measure of transmembrane helix association in a biological membrane.
W. P. Russ and D. M. Engelman (1999)
PNAS 96, 863-868
   Abstract »    Full Text »    PDF »
Mutations affecting transmembrane segment interactions impair adhesiveness of E-cadherin.
O Huber, R Kemler, and D Langosch (1999)
J. Cell Sci. 112, 4415-4423
   Abstract »    PDF »
High-Resolution Protein Design with Backbone Freedom.
P. B. Harbury, J. J. Plecs, B. Tidor, T. Alber, and P. S. Kim (1998)
Science 282, 1462-1467
   Abstract »    Full Text »
Uncoupling Hydrophobicity and Helicity in Transmembrane Segments. alpha -HELICAL PROPENSITIES OF THE AMINO ACIDS IN NON-POLAR ENVIRONMENTS.
L.-P. Liu and C. M. Deber (1998)
J. Biol. Chem. 273, 23645-23648
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Activation of Neu (ErbB-2) Mediated by Disulfide Bond-Induced Dimerization Reveals a Receptor Tyrosine Kinase Dimer Interface.
C. L. Burke and D. F. Stern (1998)
Mol. Cell. Biol. 18, 5371-5379
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Ubiquitination and Dimerization of Complement Receptor Type 2 on Sheep B Cells.
W. R. Hein, L. Dudler, W. L. Marston, T. Landsverk, A. J. Young, and D. Avila (1998)
J. Immunol. 161, 458-466
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Dimerization of the Polymeric Immunoglobulin Receptor Controls Its Transcytotic Trafficking.
K. L. Singer and K. E. Mostov (1998)
Mol. Biol. Cell 9, 901-915
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The transmembrane domain in viral fusion: Essential role for a conserved glycine residue in vesicular stomatitis virus G protein.
D. Z. Cleverley and J. Lenard (1998)
PNAS 95, 3425-3430
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Structure-based prediction of the stability of transmembrane helix-helix interactions: The sequence dependence of glycophorin A dimerization.
K. R. MacKenzie and D. M. Engelman (1998)
PNAS 95, 3583-3590
   Abstract »    Full Text »    PDF »
A Cellular Model for Long QT Syndrome. TRAPPING OF HETEROMULTIMERIC COMPLEXES CONSISTING OF TRUNCATED Kv1.1 POTASSIUM CHANNEL POLYPEPTIDES AND NATIVE Kv1.4 AND Kv1.5 CHANNELS IN THE ENDOPLASMIC RETICULUM.
E. Folco, R. Mathur, Y. Mori, P. Buckett, and G. Koren (1997)
J. Biol. Chem. 272, 26505-26510
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Peptide Mimics of the M13 Coat Protein Transmembrane Segment. RETENTION OF HELIX-HELIX INTERACTION MOTIFS.
C. Wang and C. M. Deber (2000)
J. Biol. Chem. 275, 16155-16159
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Insertion and Organization within Membranes of the delta -Endotoxin Pore-forming Domain, Helix 4-Loop-Helix 5, and Inhibition of Its Activity by a Mutant Helix 4 Peptide.
D. Gerber and Y. Shai (2000)
J. Biol. Chem. 275, 23602-23607
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