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Science 26 November 1993:
Vol. 262. no. 5138, pp. 1401 - 1407
DOI: 10.1126/science.8248779

Articles

Science, Vol 262, Issue 5138, 1401-1407
Copyright © 1993 by American Association for the Advancement of Science


articles

A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants

PB Harbury, T Zhang, PS Kim, and T Alber

Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115.

Coiled-coil sequences in proteins consist of heptad repeats containing two characteristic hydrophobic positions. The role of these buried hydrophobic residues in determining the structures of coiled coils was investigated by studying mutants of the GCN4 leucine zipper. When sets of buried residues were altered, two-, three-, and four-helix structures were formed. The x-ray crystal structure of the tetramer revealed a parallel, four-stranded coiled coil. In the tetramer conformation, the local packing geometry of the two hydrophobic positions in the heptad repeat is reversed relative to that in the dimer. These studies demonstrate that conserved, buried residues in the GCN4 leucine zipper direct dimer formation. In contrast to proposals that the pattern of hydrophobic and polar amino acids in a protein sequence is sufficient to determine three-dimensional structure, the shapes of buried side chains in coiled coils are essential determinants of the global fold.


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The Skn7 Response Regulator of Saccharomyces cerevisiae Interacts with Hsf1 In Vivo and Is Required for the Induction of Heat Shock Genes by Oxidative Stress.
D. C. Raitt, A. L. Johnson, A. M. Erkine, K. Makino, B. Morgan, D. S. Gross, and L. H. Johnston (2000)
Mol. Biol. Cell 11, 2335-2347
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Efficient Particle Production by Minimal Gag Constructs Which Retain the Carboxy-Terminal Domain of Human Immunodeficiency Virus Type 1 Capsid-p2 and a Late Assembly Domain.
M. A. Accola, B. Strack, and H. G. Göttlinger (2000)
J. Virol. 74, 5395-5402
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Characterization of Stable, Soluble Trimers Containing Complete Ectodomains of Human Immunodeficiency Virus Type 1 Envelope Glycoproteins.
X. Yang, M. Farzan, R. Wyatt, and J. Sodroski (2000)
J. Virol. 74, 5716-5725
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Modifications That Stabilize Human Immunodeficiency Virus Envelope Glycoprotein Trimers in Solution.
X. Yang, L. Florin, M. Farzan, P. Kolchinsky, P. D. Kwong, J. Sodroski, and R. Wyatt (2000)
J. Virol. 74, 4746-4754
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A Distinct Seven-residue Trigger Sequence Is Indispensable for Proper Coiled-coil Formation of the Human Macrophage Scavenger Receptor Oligomerization Domain.
S. Frank, A. Lustig, T. Schulthess, J. Engel, and R. A. Kammerer (2000)
J. Biol. Chem. 275, 11672-11677
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The retro-GCN4 leucine zipper sequence forms a stable three-dimensional structure.
P. R. E. Mittl, C. Deillon, D. Sargent, N. Liu, S. Klauser, R. M. Thomas, B. Gutte, and M. G. Grutter (2000)
PNAS 97, 2562-2566
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A Chimeric Protein Containing the N Terminus of the Adeno-Associated Virus Rep Protein Recognizes Its Target Site in an In Vivo Assay.
T. Cathomen, D. Collete, and M. D. Weitzman (2000)
J. Virol. 74, 2372-2382
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Diabetes-associated mutations in a beta -cell transcription factor destabilize an antiparallel "mini-zipper" in a dimerization interface.
Q.-X. Hua, M. Zhao, N. Narayana, S. H. Nakagawa, W. Jia, and M. A. Weiss (2000)
PNAS 97, 1999-2004
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Linker Scanning Analysis of TBP Promoter Binding Factor DNA Binding, Activation, and Repression Domains.
L. Chen and E. Bateman (2000)
J. Biol. Chem. 275, 2771-2776
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