PDBsum entry: 1dgc

Transcription/DNA

PDB-id

1dgc


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DNA/RNA

* Residue conservation analysis

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PDB id:

1dgc

Name:

Transcription/DNA

Title:

The x-ray structure of the gcn4-bzip bound to atf/creb site DNA shows the complex depends on DNA flexibility

Structure:

DNA (5'- d( Tp Gp Gp Ap Gp Ap Tp Gp Ap Cp Gp Tp Cp Ap Tp Cp T p Cp C)-3'). Chain: b. Engineered: yes. Protein (gcn4). Chain: a

Source:

Synthetic: yes. Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932

UniProt:

P03069 (GCN4_YEAST)

Seq:

Struc:

Seq:

281 a.a.

Struc:

55 a.a.

Key:		PfamA domain
		Secondary structure			CATH domain

Resolution:

3.00Å

R-factor:

0.216

Authors:

P.Koenig,T.J.Richmond

Key ref:

P.König and T.J.Richmond (1993). The X-ray structure of the GCN4-bZIP bound to ATF/CREB site DNA shows the complex depends on DNA flexibility.. J Mol Biol, 233, 139-154. [PubMed id: 8377181] [DOI: 10.1006/jmbi.1993.1490]

Date:

15-Jul-93

Release date:

22-Jun-94

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Key reference

DOI no: 10.1006/jmbi.1993.1490 J Mol Biol 233:139-154 (1993)

PubMed id: 8377181

The X-ray structure of the GCN4-bZIP bound to ATF/CREB site DNA shows the complex depends on DNA flexibility.

P.König, T.J.Richmond.

ABSTRACT

The X-ray structure of the DNA binding domain of the yeast transcriptional activator protein GCN4 bound to a DNA fragment containing the sequence of the perfectly symmetrical ATF/CREB site has been solved to 3.0 A resolution. The architecture of this specific recognition complex supports the current model for bZIP proteins: a homodimer of parallel alpha-helices form an interhelix coiled-coil region via the leucine zipper, and the two N-terminal basic regions fit into the major groove of half sites on opposite sides of the DNA double helix. The structure shows that DNA flexibility plays the predominant role in the preservation of protein contacts with the symmetric ATF/CREB site (ATGACGTCAT) as compared to the pseudo-symmetric AP-1 target site (ATGACTCAT), overcoming the positional displacement of functional groups introduced by the additional G.C base-pair at the center of the ATF/CREB sequence.

Literature references that cite this PDB file's key reference

PubMed id Reference

19468044 K.Yokoyama, H.Nogami, M.Kabasawa, S.Ebihara, A.Shimowasa, K.Hashimoto, T.Kawashima, S.A.Ishijima, and M.Suzuki (2009).
The DNA-recognition mode shared by archaeal feast/famine-regulatory proteins revealed by the DNA-binding specificities of TvFL3, FL10, FL11 and Ss-LrpB.

Nucleic Acids Res, 37, 4407-4419.

18256940 H.J.Wu, J.Luo, N.Wu, K.Matand, L.J.Zhang, X.F.Han, and B.J.Yang (2008).
Cloning, sequence and functional analysis of goat ATP-binding cassette transporter G2 (ABCG2).

Mol Biotechnol, 39, 21-27.

18949049 H.K.Chow, J.Xu, S.H.Shahravan, A.T.De Jong, G.Chen, and J.A.Shin (2008).
Hybrids of the bHLH and bZIP protein motifs display different DNA-binding activities in vivo vs. in vitro.

PLoS ONE, 3, e3514.

17559081 H.Pham, B.Chong, R.Vincenti, and L.W.Slice (2008).
Ang II and EGF synergistically induce COX-2 expression via CREB in intestinal epithelial cells.

J Cell Physiol, 214, 96.

18214959 S.Saito, T.Yokoyama, T.Aizawa, K.Kawaguchi, T.Yamaki, D.Matsumoto, T.Kamijima, M.Kamiya, Y.Kumaki, M.Mizuguchi, S.Takiya, M.Demura, and K.Kawano (2008).
Structural properties of the DNA-bound form of a novel tandem repeat DNA-binding domain, STPR.

Proteins, 72, 414-426.

17261584 M.K.Yoon, H.M.Kim, G.Choi, J.O.Lee, and B.S.Choi (2007).
Structural basis for the conformational integrity of the Arabidopsis thaliana HY5 leucine zipper homodimer.

J Biol Chem, 282, 12989-13002.

PDB code: 2oqq

16880509 B.Miotto, and K.Struhl (2006).
Differential gene regulation by selective association of transcriptional coactivators and bZIP DNA-binding domains.

Mol Cell Biol, 26, 5969-5982.

16973898 R.J.McDonald, J.D.Kahn, and L.J.Maher (2006).
DNA bending by bHLH charge variants.

Nucleic Acids Res, 34, 4846-4856.

16758500 S.Son, I.C.Tanrikulu, and D.A.Tirrell (2006).
Stabilization of bzip peptides through incorporation of fluorinated aliphatic residues.

Chembiochem, 7, 1251-1257.

15939933 A.Kanhere, and M.Bansal (2005).
Structural properties of promoters: similarities and differences between prokaryotes and eukaryotes.

Nucleic Acids Res, 33, 3165-3175.

15701809 K.Dementhon, and S.J.Saupe (2005).
DNA-binding specificity of the IDI-4 basic leucine zipper factor of Podospora anserina defined by systematic evolution of ligands by exponential enrichment (SELEX).

Eukaryot Cell, 4, 476-483.

15459288 A.I.Dragan, Y.Liu, E.N.Makeyeva, and P.L.Privalov (2004).
DNA-binding domain of GCN4 induces bending of both the ATF/CREB and AP-1 binding sites of DNA.

Nucleic Acids Res, 32, 5192-5197.

15388801 C.Guarnaccia, B.Raman, S.Zahariev, A.Simoncsits, and S.Pongor (2004).
DNA-mediated assembly of weakly interacting DNA-binding protein subunits: in vitro recruitment of phage 434 repressor and yeast GCN4 DNA-binding domains.

Nucleic Acids Res, 32, 4992-5002.

15510218 D.Panne, T.Maniatis, and S.C.Harrison (2004).
Crystal structure of ATF-2/c-Jun and IRF-3 bound to the interferon-beta enhancer.

EMBO J, 23, 4384-4393.

PDB code: 1t2k

15342915 H.Cha-Molstad, D.M.Keller, G.S.Yochum, S.Impey, and R.H.Goodman (2004).
Cell-type-specific binding of the transcription factor CREB to the cAMP-response element.

Proc Natl Acad Sci U S A, 101, 13572-13577.

15341644 K.Dementhon, S.J.Saupe, and C.Clavé (2004).
Characterization of IDI-4, a bZIP transcription factor inducing autophagy and cell death in the fungus Podospora anserina.

Mol Microbiol, 53, 1625-1640.

14704272 S.Dai, Z.Zhang, S.Chen, and R.N.Beachy (2004).
RF2b, a rice bZIP transcription activator, interacts with RF2a and is involved in symptom development of rice tungro disease.

Proc Natl Acad Sci U S A, 101, 687-692.

12578822 M.Miller, J.D.Shuman, T.Sebastian, Z.Dauter, and P.F.Johnson (2003).
Structural basis for DNA recognition by the basic region leucine zipper transcription factor CCAAT/enhancer-binding protein alpha.

J Biol Chem, 278, 15178-15184.

PDB code: 1nwq

12609888 X.Wang, W.Cao, A.Cao, and L.Lai (2003).
Thermodynamic characterization of the folding coupled DNA binding by the monomeric transcription activator GCN4 peptide.

Biophys J, 84, 1867-1875.

12209468 G.H.Bird, A.R.Lajmi, and J.A.Shin (2002).
Sequence-specific recognition of DNA by hydrophobic, alanine-rich mutants of the basic region/leucine zipper motif investigated by fluorescence anisotropy.

Biopolymers, 65, 10-20.

12381856 J.J.Hollenbeck, D.L.McClain, and M.G.Oakley (2002).
The role of helix stabilizing residues in GCN4 basic region folding and DNA binding.

Protein Sci, 11, 2740-2747.

12056905 P.R.Hardwidge, J.Wu, S.L.Williams, K.M.Parkhurst, L.J.Parkhurst, and L.J.Maher (2002).
DNA bending by bZIP charge variants: a unified study using electrophoretic phasing and fluorescence resonance energy transfer.

Biochemistry, 41, 7732-7742.

11841208 T.Morii, S.Sato, M.Hagihara, Y.Mori, K.Imoto, and K.Makino (2002).
Structure-based design of a leucine zipper protein with new DNA contacting region.

Biochemistry, 41, 2177-2183.

11180561 A.P.Demchenko (2001).
Recognition between flexible protein molecules: induced and assisted folding.

J Mol Recognit, 14, 42-61.

11113177 A.Pascual-Ahuir, R.Serrano, and M.Proft (2001).
The Sko1p repressor and Gcn4p activator antagonistically modulate stress-regulated transcription in Saccharomyces cerevisiae.

Mol Cell Biol, 21, 16-25.

11297428 H.Matsuno, K.Niikura, and Y.Okahata (2001).
Design and characterization of asparagine- and lysine-containing alanine-based helical peptides that bind selectively to A.T base pairs of oligonucleotides immobilized on a 27 mhz quartz crystal microbalance.

Biochemistry, 40, 3615-3622.

11504868 J.K.Montclare, L.S.Sloan, and A.Schepartz (2001).
Electrostatic control of half-site spacing preferences by the cyclic AMP response element-binding protein CREB.

Nucleic Acids Res, 29, 3311-3319.

11223533 J.Mazlo, R.L.Stanfield, I.A.Wilson, S.H.Hinrichs, and J.J.Stezowski (2001).
Preliminary X-ray diffraction studies of the transcriptional inhibitory antibody Fab41.4.

Acta Crystallogr D Biol Crystallogr, 57, 462-464.

11668539 J.W.Chin, and A.Schepartz (2001).
Design and Evolution of a Miniature Bcl-2 Binding Protein We thank the HHMI Biopolymer/Keck Foundation Biotechnology Resource Laboratory (Yale University School of Medicine, New Haven, CT) for oligonucleotide and peptide synthesis and amino acid analysis and Professor Jennifer Doudna (Yale University) for use of a Perseptive Voyager-DE (MALDI-TOF) mass spectrometer. We are grateful also to Dr. Junying Yuan and Dr. Alexi Degterev (Harvard Medical School) for a generous gift of Bcl-X(L)-His(6) and Stacey E. Rutledge for helpful comments. This work was supported by the National Institutes of Health.

Angew Chem Int Ed Engl, 40, 3806-3809.

11179227 M.Dlakić, A.V.Grinberg, D.A.Leonard, and T.K.Kerppola (2001).
DNA sequence-dependent folding determines the divergence in binding specificities between Maf and other bZIP proteins.

EMBO J, 20, 828-840.

11722549 Y.Sibéril, P.Doireau, and P.Gantet (2001).
Plant bZIP G-box binding factors. Modular structure and activation mechanisms.

Eur J Biochem, 268, 5655-5666.

11258889 Y.Tang, G.Ghirlanda, N.Vaidehi, J.Kua, D.T.Mainz, W.A.Goddard III, W.F.DeGrado, and D.A.Tirrell (2001).
Stabilization of coiled-coil peptide domains by introduction of trifluoroleucine.

Biochemistry, 40, 2790-2796.

11028047 A.M.Caamaño, M.E.Vázquez, J.Martínez-Costas, L.Castedo, and J.L.Mascareñas (2000).
A Light-Modulated Sequence-Specific DNA-Binding Peptide This work was supported by the Spanish M.E.C. (PB97-0524) and the Xunta de Galicia (XUGA 20906B96). A.M.C and E.V. thank the Xunta de Galicia and the University of Santiago for their predoctoral fellowships. We are grateful to Prof. M. Mosquera and Prof. J. Benavente for allowing us to use the spectrofluorimetry and radioactivity facilities, respectively, and to Dr. Chris Abell (Cambridge University, Iberdrola Visiting Professor at the University of Santiago) for critical reading of the manuscript.

Angew Chem Int Ed Engl, 39, 3104-3107.

11754342 I.Lafontaine, and R.Lavery (2000).
ADAPT: a molecular mechanics approach for studying the structural properties of long DNA sequences.

Biopolymers, 56, 292-310.

10886376 J.Usukura, Y.Nishizawa, A.Shimomura, K.Kobayashi, T.Nagatsu, and M.Hagiwara (2000).
Direct imaging of phosphorylation-dependent conformational change and DNA binding of CREB by electron microscopy.

Genes Cells, 5, 515-522.

10940257 L.D.Williams, and L.J.Maher (2000).
Electrostatic mechanisms of DNA deformation.

Annu Rev Biophys Biomol Struct, 29, 497-521.

10567395 A.L.Kimzey, and W.S.Dynan (1999).
Identification of a human T-cell leukemia virus type I tax peptide in contact with DNA.

J Biol Chem, 274, 34226-34232.

10574952 J.M.Bosilevac, R.J.Olsen, J.A.Bridge, and S.H.Hinrichs (1999).
Tumor cell viability in clear cell sarcoma requires DNA binding activity of the EWS/ATF1 fusion protein.

J Biol Chem, 274, 34811-34818.

10026254 K.Suzuki, T.Yamada, and T.Tanaka (1999).
Role of the buried glutamate in the alpha-helical coiled coil domain of the macrophage scavenger receptor.

Biochemistry, 38, 1751-1756.

9593719 A.L.Kimzey, and W.S.Dynan (1998).
Specific regions of contact between human T-cell leukemia virus type I Tax protein and DNA identified by photocross-linking.

J Biol Chem, 273, 13768-13775.

9465027 A.Sitlani, and D.M.Crothers (1998).
DNA-binding domains of Fos and Jun do not induce DNA curvature: an investigation with solution and gel methods.

Proc Natl Acad Sci U S A, 95, 1404-1409.

9668114 J.R.Lundblad, R.P.Kwok, M.E.Laurance, M.S.Huang, J.P.Richards, R.G.Brennan, and R.H.Goodman (1998).
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 Biol Chem, 273, 19251-19259.

9580678 L.A.Tomky, J.K.Strauss-Soukup, and L.J.Maher (1998).
Effects of phosphate neutralization on the shape of the AP-1 transcription factor binding site in duplex DNA.

Nucleic Acids Res, 26, 2298-2305.

9585522 L.S.Sloan, and A.Schepartz (1998).
Sequence determinants of the intrinsic bend in the cyclic AMP response element.

Biochemistry, 37, 7113-7118.

9668115 M.K.Shirra, and U.Hansen (1998).
LSF and NTF-1 share a conserved DNA recognition motif yet require different oligomerization states to form a stable protein-DNA complex.

J Biol Chem, 273, 19260-19268.

9465028 S.C.Hockings, J.D.Kahn, and D.M.Crothers (1998).
Characterization of the ATF/CREB site and its complex with GCN4.

Proc Natl Acad Sci U S A, 95, 1410-1415.

9737882 S.Weber-Bornhauser, J.Eggenberger, I.Jelesarov, A.Bernard, C.Berger, and H.R.Bosshard (1998).
Thermodynamics and kinetics of the reaction of a single-chain antibody fragment (scFv) with the leucine zipper domain of transcription factor GCN4.

Biochemistry, 37, 13011-13020.

9694827 X.Wu, C.Spiro, W.G.Owen, and C.T.McMurray (1998).
cAMP response element-binding protein monomers cooperatively assemble to form dimers on DNA.

J Biol Chem, 273, 20820-20827.

9548952 Y.Okahata, K.Niikura, Y.Sugiura, M.Sawada, and T.Morii (1998).
Kinetic studies of sequence-specific binding of GCN4-bZIP peptides to DNA strands immobilized on a 27-MHz quartz-crystal microbalance.

Biochemistry, 37, 5666-5672.

9765261 Y.Tang, F.Tie, I.Boros, R.Harrod, M.Glover, and C.Z.Giam (1998).
An extended alpha-helix and specific amino acid residues opposite the DNA-binding surface of the cAMP response element binding protein basic domain are important for human T cell lymphotropic retrovirus type I Tax binding.

J Biol Chem, 273, 27339-27346.

9303538 A.S.Carroll, D.E.Gilbert, X.Liu, J.W.Cheung, J.E.Michnowicz, G.Wagner, T.E.Ellenberger, and T.K.Blackwell (1997).
SKN-1 domain folding and basic region monomer stabilization upon DNA binding.

Genes Dev, 11, 2227-2238.

9016600 A.V.Kralicek, P.K.Wilson, G.B.Ralston, R.G.Wake, and G.F.King (1997).
Reorganization of terminator DNA upon binding replication terminator protein: implications for the functional replication fork arrest complex.

Nucleic Acids Res, 25, 590-596.

9144164 D.A.Leonard, N.Rajaram, and T.K.Kerppola (1997).
Structural basis of DNA bending and oriented heterodimer binding by the basic leucine zipper domains of Fos and Jun.

Proc Natl Acad Sci U S A, 94, 4913-4918.

9254598 D.N.Paolella, Y.Liu, M.A.Fabian, and A.Schepartz (1997).
Electrostatic mechanism for DNA bending by bZIP proteins.

Biochemistry, 36, 10033-10038.

9241421 G.Patikoglou, and S.K.Burley (1997).
Eukaryotic transcription factor-DNA complexes.

Annu Rev Biophys Biomol Struct, 26, 289-325.

8993335 H.Wendt, L.Leder, H.Härmä, I.Jelesarov, A.Baici, and H.R.Bosshard (1997).
Very rapid, ionic strength-dependent association and folding of a heterodimeric leucine zipper.

Biochemistry, 36, 204-213.

9303004 K.Swaminathan, P.Flynn, R.J.Reece, and R.Marmorstein (1997).
Crystal structure of a PUT3-DNA complex reveals a novel mechanism for DNA recognition by a protein containing a Zn2Cys6 binuclear cluster.

Nat Struct Biol, 4, 751-759.

PDB code: 1zme

9372930 L.Fernandes, C.Rodrigues-Pousada, and K.Struhl (1997).
Yap, a novel family of eight bZIP proteins in Saccharomyces cerevisiae with distinct biological functions.

Mol Cell Biol, 17, 6982-6993.

9380502 M.R.Conte, A.N.Lane, and G.Bloomberg (1997).
Solution structure of the ATF-2 recognition site and its interaction with the ATF-2 peptide.

Nucleic Acids Res, 25, 3808-3815.

PDB code: 1saa

9782775 M.Tateno, K.Yamasaki, N.Amano, J.Kakinuma, H.Koike, M.D.Allen, and M.Suzuki (1997).
DNA recognition by beta-sheets.

Biopolymers, 44, 335-359.

9782776 R.E.Dickerson, and T.K.Chiu (1997).
Helix bending as a factor in protein/DNA recognition.

Biopolymers, 44, 361-403.

9033590 S.J.Metallo, and A.Schepartz (1997).
Certain bZIP peptides bind DNA sequentially as monomers and dimerize on the DNA.

Nat Struct Biol, 4, 115-117.

9224594 S.J.Metallo, D.N.Paolella, and A.Schepartz (1997).
The role of a basic amino acid cluster in target site selection and non-specific binding of bZIP peptides to DNA.

Nucleic Acids Res, 25, 2967-2972.

9184234 T.K.Kerppola, and T.Curran (1997).
The transcription activation domains of Fos and Jun induce DNA bending through electrostatic interactions.

EMBO J, 16, 2907-2916.

9053397 W.D.Kohn, C.T.Mant, and R.S.Hodges (1997).
Alpha-helical protein assembly motifs.

J Biol Chem, 272, 2583-2586.

9108036 X.Zeng, A.M.Herndon, and J.C.Hu (1997).
Buried asparagines determine the dimerization specificities of leucine zipper mutants.

Proc Natl Acad Sci U S A, 94, 3673-3678.

9336844 X.Zeng, H.Zhu, H.A.Lashuel, and J.C.Hu (1997).
Oligomerization properties of GCN4 leucine zipper e and g position mutants.

Protein Sci, 6, 2218-2226.

11725111 C.A.Gilchrist, D.J.Orten, and S.H.Hinrichs (1996).
Evidence for the Role of Cyclic AMP-Responsive Elements in Human Virus Replication and Disease.

J Biomed Sci, 3, 293-306.

8942664 C.Berger, I.Jelesarov, and H.R.Bosshard (1996).
Coupled folding and site-specific binding of the GCN4-bZIP transcription factor to the AP-1 and ATF/CREB DNA sites studied by microcalorimetry.

Biochemistry, 35, 14984-14991.

8631313 D.Garcia de Viedma, R.Giraldo, G.Rivas, E.Fernández-Tresguerres, and R.Diaz-Orejas (1996).
A leucine zipper motif determines different functions in a DNA replication protein.

EMBO J, 15, 925-934.

8654420 D.Krebs, B.Dahmani, M.Monnot, O.Mauffret, F.Troalen, and S.Fermandjian (1996).
Dissection of the basic subdomain of the c-Jun oncoprotein: a structural analysis of two peptide fragments by CD, Fourier-transform infrared and NMR.

Eur J Biochem, 235, 699-712.

8662824 F.K.Junius, S.I.O'Donoghue, M.Nilges, A.S.Weiss, and G.F.King (1996).
High resolution NMR solution structure of the leucine zipper domain of the c-Jun homodimer.

J Biol Chem, 271, 13663-13667.

PDB code: 1jun

8842252 G.F.King (1996).
NMR spectroscopy and X-ray crystallography provide complementary information on the structure and dynamics of leucine zippers.

Biophys J, 71, 1152-1154.

8810925 H.Chao, M.E.Houston, S.Grothe, C.M.Kay, M.O'Connor-McCourt, R.T.Irvin, and R.S.Hodges (1996).
Kinetic study on the formation of a de novo designed heterodimeric coiled-coil: use of surface plasmon resonance to monitor the association and dissociation of polypeptide chains.

Biochemistry, 35, 12175-12185.

8703910 K.H.Heuer, J.P.Mackay, P.Podzebenko, N.P.Bains, A.S.Weiss, G.F.King, and S.B.Easterbrook-Smith (1996).
Development of a sensitive peptide-based immunoassay: application to detection of the Jun and Fos oncoproteins.

Biochemistry, 35, 9069-9075.

8948639 M.John, R.Leppik, S.J.Busch, M.Granger-Schnarr, and M.Schnarr (1996).
DNA binding of Jun and Fos bZip domains: homodimers and heterodimers induce a DNA conformational change in solution.

Nucleic Acids Res, 24, 4487-4494.

8567657 M.Olive, S.C.Williams, C.Dezan, P.F.Johnson, and C.Vinson (1996).
Design of a C/EBP-specific, dominant-negative bZIP protein with both inhibitory and gain-of-function properties.

J Biol Chem, 271, 2040-2047.

8599943 M.Suckow, M.Lopata, A.Seydel, B.Kisters-Woike, B.von Wilcken-Bergmann, and B.Müller-Hill (1996).
Mutant bZip-DNA complexes with four quasi-identical protein-DNA interfaces.

EMBO J, 15, 598-606.

8663440 S.Witte, F.Neumann, U.Krawinkel, and M.Przybylski (1996).
Mass spectrometric identification of leucine zipper-like homodimer complexes of the autoantigen L7.

J Biol Chem, 271, 18171-18175.

8610143 T.Sera, and P.G.Schultz (1996).
In vivo selection of basic region-leucine zipper proteins with altered DNA-binding specificities.

Proc Natl Acad Sci U S A, 93, 2920-2925.

7479080 B.Koldin, M.Suckow, A.Seydel, B.von Wilcken-Bergmann, and B.Müller-Hill (1995).
A comparison of the different DNA binding specificities of the bZip proteins C/EBP and GCN4.

Nucleic Acids Res, 23, 4162-4169.

7635148 D.Krebs, B.Dahmani, S.el Antri, M.Monnot, O.Convert, O.Mauffret, F.Troalen, and S.Fermandjian (1995).
The basic subdomain of the c-Jun oncoprotein. A joint CD, Fourier-transform infrared and NMR study.

Eur J Biochem, 231, 370-380.

7664107 D.Stanojevic, and G.L.Verdine (1995).
Deconstruction of GCN4/GCRE into a monomeric peptide-DNA complex.

Nat Struct Biol, 2, 450-457.

7885838 D.V.Kuprash, N.R.Rice, and S.A.Nedospasov (1995).
Homodimer of p50 (NF kappa B1) does not introduce a substantial directed bend into DNA according to three different experimental assays.

Nucleic Acids Res, 23, 427-433.

7601148 H.Baumann, and T.Härd (1995).
Structural characterization of a short peptide fragment that mediates estrogen-receptor dimerization.

Eur J Biochem, 230, 879-885.

8520482 H.Wendt, E.Dürr, R.M.Thomas, M.Przybylski, and H.R.Bosshard (1995).
Characterization of leucine zipper complexes by electrospray ionization mass spectrometry.

Protein Sci, 4, 1563-1570.

7568206 J.C.Becker, A.Nikroo, T.Brabletz, and R.A.Reisfeld (1995).
DNA loops induced by cooperative binding of transcriptional activator proteins and preinitiation complexes.

Proc Natl Acad Sci U S A, 92, 9727-9731.

7630732 J.Kim, and K.Struhl (1995).
Determinants of half-site spacing preferences that distinguish AP-1 and ATF/CREB bZIP domains.

Nucleic Acids Res, 23, 2531-2537.

8749848 M.Suzuki, and M.Gerstein (1995).
Binding geometry of alpha-helices that recognize DNA.

Proteins, 23, 525-535.

7610037 M.Suzuki, and N.Yagi (1995).
Stereochemical basis of DNA bending by transcription factors.

Nucleic Acids Res, 23, 2083-2091.

7891686 N.B.Haas, C.A.Cantwell, P.F.Johnson, and J.B.Burch (1995).
DNA-binding specificity of the PAR basic leucine zipper protein VBP partially overlaps those of the C/EBP and CREB/ATF families and is influenced by domains that flank the core basic region.

Mol Cell Biol, 15, 1923-1932.

7621832 P.Percipalle, A.Simoncsits, S.Zakhariev, C.Guarnaccia, R.Sánchez, and S.Pongor (1995).
Rationally designed helix-turn-helix proteins and their conformational changes upon DNA binding.

EMBO J, 14, 3200-3205.

8750235 V.V.Svetlov, and T.G.Cooper (1995).
Review: compilation and characteristics of dedicated transcription factors in Saccharomyces cerevisiae.

Yeast, 11, 1439-1484.

8026470 D.Krylov, I.Mikhailenko, and C.Vinson (1994).
A thermodynamic scale for leucine zipper stability and dimerization specificity: e and g interhelical interactions.

EMBO J, 13, 2849-2861.

8041727 L.Nekludova, and C.O.Pabo (1994).
Distinctive DNA conformation with enlarged major groove is found in Zn-finger-DNA and other protein-DNA complexes.

Proc Natl Acad Sci U S A, 91, 6948-6952.

8041795 L.R.Patel, T.Curran, and T.K.Kerppola (1994).
Energy transfer analysis of Fos-Jun dimerization and DNA binding.

Proc Natl Acad Sci U S A, 91, 7360-7364.

8036145 M.Suckow, A.Madan, B.Kisters-Woike, B.von Wilcken-Bergmann, and B.Müller-Hill (1994).
Creating new DNA binding specificities in the yeast transcriptional activator GCN4 by combining selected amino acid substitutions.

Nucleic Acids Res, 22, 2198-2208.

7971270 M.Suckow, K.Schwamborn, B.Kisters-Woike, B.von Wilcken-Bergmann, and B.Müller-Hill (1994).
Replacement of invariant bZip residues within the basic region of the yeast transcriptional activator GCN4 can change its DNA binding specificity.

Nucleic Acids Res, 22, 4395-4404.

7809040 M.Suzuki, and N.Yagi (1994).
DNA recognition code of transcription factors in the helix-turn-helix, probe helix, hormone receptor, and zinc finger families.

Proc Natl Acad Sci U S A, 91, 12357-12361.

8197144 N.P.Johnson, J.Lindstrom, W.A.Baase, and P.H.von Hippel (1994).
Double-stranded DNA templates can induce alpha-helical conformation in peptides containing lysine and alanine: functional implications for leucine zipper and helix-loop-helix transcription factors.

Proc Natl Acad Sci U S A, 91, 4840-4844.

7656043 S.K.Burley (1994).
Plus ça change, plus c'est la même chose.

Nat Struct Biol, 1, 207-208.

7800488 X.Niu, and M.J.Guiltinan (1994).
DNA binding specificity of the wheat bZIP protein EmBP-1.

Nucleic Acids Res, 22, 4969-4978.

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.