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Science 25 October 1991: Vol. 254. no. 5031, pp. 539 - 544 DOI: 10.1126/science.1948029
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Articles
Science, Vol 254, Issue 5031, 539-544
Copyright © 1991 by American Association for the Advancement of Science
X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil
EK O'Shea,
JD Klemm,
PS Kim,
and
T Alber
Howard Hughes Medical Institute, Cambridge, MA 02142.
The x-ray crystal structure of a peptide corresponding to the leucine zipper of the yeast transcriptional activator GCN4 has been determined at 1.8 angstrom resolution. The peptide forms a parallel, two-stranded coiled coil of alpha helices packed as in the "knobs-into-holes" model proposed by Crick in 1953. Contacts between the helices include ion pairs and an extensive hydrophobic interface that contains a distinctive hydrogen bond. The conserved leucines, like the residues in the alternate hydrophobic repeat, make side-to-side interactions (as in a handshake) in every other layer of the dimer interface. The crystal structure of the GCN4 leucine zipper suggests a key role for the leucine repeat, but also shows how other features of the coiled coil contribute to dimer formation.
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- Multimer Formation Is Not Essential for Nuclear Export of Human T-Cell Leukemia Virus Type 1 Rex trans-Activator Protein.
- P. Heger, O. Rosorius, C. Koch, G. Casari, R. Grassmann, and J. Hauber (1998)
J. Virol.
72, 8659-8668
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- Isolation and Characterization of Two Proteins from Moraxella catarrhalis That Bear a Common Epitope.
- J. C. McMichael, M. J. Fiske, R. A. Fredenburg, D. N. Chakravarti, K. R. VanDerMeid, V. Barniak, J. Caplan, E. Bortell, S. Baker, R. Arumugham, et al. (1998)
Infect. Immun.
66, 4374-4381
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- Stabilization of Human Immunodeficiency Virus Type 1 Envelope Glycoprotein Trimers by Disulfide Bonds Introduced into the gp41 Glycoprotein Ectodomain.
- M. Farzan, H. Choe, E. Desjardins, Y. Sun, J. Kuhn, J. Cao, D. Archambault, P. Kolchinsky, M. Koch, R. Wyatt, et al. (1998)
J. Virol.
72, 7620-7625
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- A method for directed evolution and functional cloning of enzymes.
- H. Pedersen, S. Holder, D. P. Sutherlin, U. Schwitter, D. S. King, and P. G. Schultz (1998)
PNAS
95, 10523-10528
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- cAMP Response Element-binding Protein Monomers Cooperatively Assemble to Form Dimers on DNA.
- X. Wu, C. Spiro, W. G. Owen, and C. T. McMurray (1998)
J. Biol. Chem.
273, 20820-20827
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- HtrI Is a Dimer Whose Interface Is Sensitive to Receptor Photoactivation and His-166 Replacements in Sensory Rhodopsin I.
- X.-N. Zhang and J. L. Spudich (1998)
J. Biol. Chem.
273, 19722-19728
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- The Human T-cell Leukemia Virus-1 Transcriptional Activator Tax Enhances cAMP-responsive Element-binding Protein (CREB) Binding Activity through Interactions with the DNA Minor Groove.
- J. R. Lundblad, R. P. S. Kwok, M. E. Laurance, M. S. Huang, J. P. Richards, R. G. Brennan, and R. H. Goodman (1998)
J. Biol. Chem.
273, 19251-19259
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- Role of the PAS Domain in Regulation of Dimerization and DNA Binding Specificity of the Dioxin Receptor.
- I. Pongratz, C. Antonsson, M. L. Whitelaw, and L. Poellinger (1998)
Mol. Cell. Biol.
18, 4079-4088
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- Tenascin-C Hexabrachion Assembly Is a Sequential Two-step Process Initiated by Coiled-coil alpha -Helices.
- R. A. Kammerer, T. Schulthess, R. Landwehr, A. Lustig, D. Fischer, and J. Engel (1998)
J. Biol. Chem.
273, 10602-10608
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- A Leucine Zipper-Like Domain Is Essential for Dimerization and Encapsidation of Bluetongue Virus Nucleocapsid Protein VP4.
- N. Ramadevi, J. Rodriguez, and P. Roy (1998)
J. Virol.
72, 2983-2990
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- Neurofilament (NF) Assembly; Divergent Characteristics of Human and Rodent NF-L Subunits.
- J. Carter, A. Gragerov, K. Konvicka, G. Elder, H. Weinstein, and R. A. Lazzarini (1998)
J. Biol. Chem.
273, 5101-5108
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- A Dominant-Negative Inhibitor of CREB Reveals that It Is a General Mediator of Stimulus-Dependent Transcription of c-fos.
- S. Ahn, M. Olive, S. Aggarwal, D. Krylov, D. D. Ginty, and C. Vinson (1998)
Mol. Cell. Biol.
18, 967-977
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