The structure of the Antennapedia homeodomain determined by NMR spectroscopy in solution: Comparison with prokaryotic repressors
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W. J. Gehring | M. Billeter | K. Wüthrich | W. Gehring | G. Otting | Y. Qian | M. Müller | M. Billeter | K. Wüthrich | M. Müller | G. Otting | Y. Q. Qian | M. Müller
[1] R. Brüschweiler,et al. Combined use of hard and soft pulses for ω1 decoupling in two-dimensional NMR spectroscopy , 1988 .
[2] J. Gillis,et al. Crystal Structure Analysis , 1960 .
[3] G. Rubin,et al. Human DNA sequences homologous to a protein coding region conserved between homeotic genes of Drosophila , 1984, Cell.
[4] M. Billeter,et al. Spatial arrangement of the three α helices in the solution conformation of E. coli lac represser DNA‐binding domain , 1984, FEBS letters.
[5] M. Scott,et al. The structure and function of the homeodomain. , 1989, Biochimica et biophysica acta.
[6] K. Wüthrich,et al. Secondary structure determination for the Antennapedia homeodomain by nuclear magnetic resonance and evidence for a helix‐turn‐helix motif. , 1988, The EMBO journal.
[7] N Go,et al. Calculation of protein conformations by proton-proton distance constraints. A new efficient algorithm. , 1985, Journal of molecular biology.
[8] Jordan,et al. Structure of the lambda complex at 2.5 A resolution: details of the repressor-operator interactions , 1988, Science.
[9] M Ptashne,et al. Recognition of a DNA operator by the repressor of phage 434: a view at high resolution , 1988, Science.
[10] William McGinnis,et al. Cloning of an X. laevis gene expressed during early embryogenesis coding for a peptide region homologous to Drosophila homeotic genes , 1984, Cell.
[11] A. Laughon,et al. Sequence of a Drosophila segmentation gene: protein structure homology with DNA-binding proteins , 1984, Nature.
[12] W. Gehring,et al. Homeo boxes in the study of development. , 1987, Science.
[13] A. Joachimiak,et al. Crystal structure of trp represser/operator complex at atomic resolution , 1988, Nature.
[14] S W Lin,et al. Vectors for selective expression of cloned DNAs by T7 RNA polymerase. , 1987, Gene.
[15] F. Studier,et al. Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. , 1986, Journal of molecular biology.
[16] B. Matthews,et al. Comparison of the structures of Cro and λ repressor proteins from bacteriophage λ , 1983 .
[17] W. Gehring,et al. Structural organization and sequence of the homeotic gene Antennapedia of Drosophila melanogaster. , 1986, The EMBO journal.
[18] C. Pabo,et al. The operator-binding domain of λ repressor: structure and DNA recognition , 1982, Nature.
[19] P. Tsonis,et al. Modeling of the homoeo domain suggests similar structure to repressors. , 1988, Biochemical and Biophysical Research Communications - BBRC.
[20] S Subbiah,et al. Structure of the amino-terminal domain of phage 434 repressor at 2.0 A resolution. , 1989, Journal of molecular biology.
[21] W. McGinnis,et al. Isolation of a homoeo box-containing gene from the engrailed region of Drosophila and the spatial distribution of its transcripts , 1985, Nature.
[22] G. A. van der Marel,et al. H NMR study of a complex between the lac repressor headpiece and a 22 base pair symmetric lac operator. , 1989, Biochemistry.
[23] W. J. Gehring,et al. A conserved DNA sequence in homoeotic genes of the Drosophila Antennapedia and bithorax complexes , 1984, Nature.
[24] S. Harrison,et al. Structure of a phage 434 Cro/DNA complex , 1988, Nature.
[25] William McGinnis,et al. Fly and frog homoeo domains show homologies with yeast mating type regulatory proteins , 1984, Nature.
[26] Michael B. Smith,et al. Homoeo-domain homology in yeast MATα2 is essential for repressor activity , 1986, Nature.
[27] William McGinnis,et al. Molecular cloning and chromosome mapping of a mouse DNA sequence homologous to homeotic genes of drosophila , 1984, Cell.
[28] A. Mclachlan. Gene duplications in the structural evolution of chymotrypsin. , 1979, Journal of molecular biology.
[29] L. Kauvar,et al. The engrailed locus of drosophila: Structural analysis of an embryonic transcript , 1985, Cell.
[30] J. Richardson,et al. The anatomy and taxonomy of protein structure. , 1981, Advances in protein chemistry.
[31] K Wüthrich,et al. Polypeptide secondary structure determination by nuclear magnetic resonance observation of short proton-proton distances. , 1984, Journal of molecular biology.
[32] M. Scott,et al. Structural relationships among genes that control development: sequence homology between the Antennapedia, Ultrabithorax, and fushi tarazu loci of Drosophila. , 1984, Proceedings of the National Academy of Sciences of the United States of America.
[33] K. Wüthrich,et al. Isolation and sequence‐specific DNA binding of the Antennapedia homeodomain. , 1988, The EMBO journal.
[34] K. Wüthrich,et al. Studies of J-connectives and selective 1H-1H Overhauser effects in H2O solutions of biological macromolecules by two-dimensional NMR experiments. , 1980, Biochemical and biophysical research communications.
[35] Werner Braun,et al. Automated stereospecific 1H NMR assignments and their impact on the precision of protein structure determinations in solution , 1989 .
[36] B. Matthews,et al. The helix-turn-helix DNA binding motif. , 1989, The Journal of biological chemistry.
[37] M. Billeter,et al. Three‐dimensional structure of the neurotoxin ATX Ia from Anemonia sulcata in aqueous solution determined by nuclear magnetic resonance spectroscopy , 1989, Proteins.
[38] Z Otwinowski,et al. Flexibility of the DNA‐binding domains of trp repressor , 1988, Proteins.
[39] K. Wüthrich,et al. Secondary structure of the lac repressor DNA-binding domain by two-dimensional 1H nuclear magnetic resonance in solution. , 1983, Proceedings of the National Academy of Sciences of the United States of America.
[40] M. Ptashne,et al. Repressor structure and the mechanism of positive control , 1983, Cell.
[41] T. Steitz,et al. Structure of catabolite gene activator protein at 2.9-A resolution. Incorporation of amino acid sequence and interactions with cyclic AMP. , 1982, The Journal of biological chemistry.
[42] K. G. Coleman,et al. The invected gene of Drosophila: sequence analysis and expression studies reveal a close kinship to the engrailed gene. , 1987, Genes & development.
[43] T. Steitz,et al. Structural similarity in the DNA-binding domains of catabolite gene activator and cro repressor proteins. , 1982, Proceedings of the National Academy of Sciences of the United States of America.
[44] B. Matthews,et al. Comparison of the structures of cro and lambda repressor proteins from bacteriophage lambda. , 1989, Journal of molecular biology.
[45] K Wüthrich,et al. Determination of the complete three-dimensional structure of the alpha-amylase inhibitor tendamistat in aqueous solution by nuclear magnetic resonance and distance geometry. , 1988, Journal of molecular biology.
[46] K Wüthrich,et al. Comparison of the high-resolution structures of the alpha-amylase inhibitor tendamistat determined by nuclear magnetic resonance in solution and by X-ray diffraction in single crystals. , 1989, Journal of molecular biology.