The winged-helix DNA-binding motif: Another helix-turn-helix takeoff
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[1] S. Burley,et al. Co-crystal structure of the HNF-3/fork head DNA-recognition motif resembles histone H5 , 1993, Nature.
[2] T. Ceska,et al. The X-ray structure of an atypical homeodomain present in the rat liver transcription factor LFB1/HNF1 and implications for DNA binding. , 1993 .
[3] K. Wüthrich,et al. The three‐dimensional NMR‐solution structure of the polypeptide fragment 195–286 of the LFB1/HNF1 transcription factor from rat liver comprises a nonclassical homeodomain. , 1993, The EMBO journal.
[4] R. Kaptein,et al. Solution structure of the POU-specific DNA-binding domain of Oct-1 , 1993, Nature.
[5] P. Wright,et al. The solution structure of the Oct-1 POU-specific domain reveals a striking similarity to the bacteriophage λ repressor DNA-binding domain , 1993, Cell.
[6] V. Ramakrishnan,et al. Crystal structure of globular domain of histone H5 and its implications for nucleosome binding , 1993, Nature.
[7] C. Wolberger. Transcription factor structure and DNA binding , 1993 .
[8] R. Brennan. DNA recognition by the helix-turn-helix motif , 1992 .
[9] J. Baldwin. Protein-nucleic acid interactions in nucleosomes , 1992 .
[10] S. Harrison,et al. A structural taxonomy of DNA-binding domains , 1991, Nature.
[11] H. Goldberg,et al. The DNA binding arm of lambda repressor: critical contacts from a flexible region. , 1991, Science.
[12] W. DeGrado,et al. DNA-induced increase in the alpha-helical content of C/EBP and GCN4. , 1991, Biochemistry.
[13] T. Steitz,et al. Crystal structure of a CAP-DNA complex: the DNA is bent by 90 degrees , 1991, Science.
[14] J. Widom. Nucleosomes and chromatin , 1991 .
[15] Carl O. Pabo,et al. Crystal structure of an engrailed homeodomain-DNA complex at 2.8 Å resolution: A framework for understanding homeodomain-DNA interactions , 1990, Cell.
[16] Kevin Struhl,et al. Folding transition in the DMA-binding domain of GCN4 on specific binding to DNA , 1990, Nature.
[17] M. Caruthers,et al. Role of the Cro repressor carboxy-terminal domain and flexible dimer linkage in operator and nonspecific DNA binding. , 1990, Biochemistry.
[18] K Wüthrich,et al. Protein–DNA contacts in the structure of a homeodomain–DNA complex determined by nuclear magnetic resonance spectroscopy in solution. , 1990, The EMBO journal.
[19] I. Dodd,et al. Improved detection of helix-turn-helix DNA-binding motifs in protein sequences. , 1990, Nucleic acids research.
[20] P. Ingham. The X, Y, Z of head development , 1990, Nature.
[21] P. Sigler,et al. The stereochemistry and biochemistry of the trp repressor-operator complex. , 1990, Biochimica et biophysica acta.
[22] S. Harrison,et al. Conserved residues make similar contacts in two repressor-operator complexes. , 1990, Science.
[23] B. Matthews,et al. The helix-turn-helix DNA binding motif. , 1989, The Journal of biological chemistry.
[24] J. Carey. trp repressor arms contribute binding energy without occupying unique locations on DNA. , 1989, The Journal of biological chemistry.
[25] A. Joachimiak,et al. Crystal structure of trp represser/operator complex at atomic resolution , 1988, Nature.
[26] C. Pabo,et al. The operator-binding domain of λ repressor: structure and DNA recognition , 1982, Nature.
[27] Thomas A. Steitz,et al. Structure of catabolite gene activator protein at 2.9 Å resolution suggests binding to left-handed B-DNA , 1981, Nature.
[28] B. Matthews,et al. Structure of the cro repressor from bacteriophage λ and its interaction with DNA , 1981, Nature.
[29] R. Sauer,et al. Transcription factors: structural families and principles of DNA recognition. , 1992, Annual review of biochemistry.
[30] Cynthia Wolberger,et al. Crystal structure of a MAT alpha 2 homeodomain-operator complex suggests a general model for homeodomain-DNA interactions. , 1991, Cell.