caa a22 4500 47713601X CHVBK 20180405111718.0 cr unu---uuuuu 170330e19971201xx s 000 0 eng 10.1023/A:1018399711996 doi (NATIONALLICENCE)springer-10.1023/A:1018399711996 Correction of the NMR structure of the ETS1/DNA complex [Elektronische Daten] [Milton Werner, G. Clore, Constance Fisher, Robert Fisher, Loc Trinh, Joseph Shiloach, Angela Gronenborn] The ETS family of transcription factors consists of a group of proteins that share a highly conserved 85 amino acid DNA-binding domain (DBD). This family recognizes a consensus sequence rich in purine bases with a central GGAA motif. A comparison of the published three-dimensional structures of the DBD/DNA complexes of ETS1 by NMR [Werner et al. (1995) Cell, 83, 761-771] and the related Pu.1 by X-ray crystallography [Kodandapani et al. (1996) Nature, 380, 456-460] reveals an apparent discrepancy in which the protein domains bind with opposite polarity to their target sequences. This surprising and highly unlikely result prompted us to reexamine our NMR structure. Additional NMR experiments now reveal an error in the original interpretation of the spectra defining the orientation of the ETS1-DBD on DNA. It was originally reported that the ETS1-DBD bound to DNA with a bipartite motif involving major groove recognition via a helix-turn-helix element and minor groove recognition via protein side-chain intercalation. The presence of intercalation was deduced on the basis of numerous NOEs between several amino acids in the protein and a resonance at 12.33 ppm originally assigned to a DNA imino proton. New NMR experiments now conclusively demonstrate that this resonance, which is located within the DNA imino proton region of the spectrum, arises from the hydroxyl proton of Tyr86. Realization of this error necessitated reanalysis of the intermolecular NOEs. This revealed that the orientation of the ETS1-DBD in the complex is opposite to that originally reported and that a tryptophan residue does not intercalate into the DNA. The calculation of a new ensemble of structures based on the corrected data indicates that the structure of the ETS1-DBD/DNA complex is indeed similar to the X-ray structure of the Pu.1-DBD/DNA complex. Kluwer Academic Publishers, 1997 ETS1/DNA complex nationallicence Solution structure nationallicence Pu.1/DNA complex nationallicence Werner Milton Laboratory of Chemical Physics, NIDDKD, National Institutes of Health, Building 5, 20892-0520, Bethesda, MD, U.S.A aut Clore G. Laboratory of Chemical Physics, NIDDKD, National Institutes of Health, Building 5, 20892-0520, Bethesda, MD, U.S.A aut Fisher Constance Frederick Cancer Research and Development Center, National Cancer Institute, 21707, Frederick, MD, U.S.A aut Fisher Robert Frederick Cancer Research and Development Center, National Cancer Institute, 21707, Frederick, MD, U.S.A aut Trinh Loc Laboratory of Cellular and Developmental Biology, NIDDKD, 20895-0520, Bethesda, MD, U.S.A aut Shiloach Joseph Laboratory of Cellular and Developmental Biology, NIDDKD, 20895-0520, Bethesda, MD, U.S.A aut Gronenborn Angela Laboratory of Chemical Physics, NIDDKD, National Institutes of Health, Building 5, 20892-0520, Bethesda, MD, U.S.A aut Journal of Biomolecular NMR Kluwer Academic Publishers 10/4(1997-12-01), 317-328 0925-2738 10:4<317 1997 10 10858 https://doi.org/10.1023/A:1018399711996 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1023/A:1018399711996 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Werner Milton Laboratory of Chemical Physics, NIDDKD, National Institutes of Health, Building 5, 20892-0520, Bethesda, MD, U.S.A aut NATIONALLICENCE 700 1- Clore G. Laboratory of Chemical Physics, NIDDKD, National Institutes of Health, Building 5, 20892-0520, Bethesda, MD, U.S.A aut NATIONALLICENCE 700 1- Fisher Constance Frederick Cancer Research and Development Center, National Cancer Institute, 21707, Frederick, MD, U.S.A aut NATIONALLICENCE 700 1- Fisher Robert Frederick Cancer Research and Development Center, National Cancer Institute, 21707, Frederick, MD, U.S.A aut NATIONALLICENCE 700 1- Trinh Loc Laboratory of Cellular and Developmental Biology, NIDDKD, 20895-0520, Bethesda, MD, U.S.A aut NATIONALLICENCE 700 1- Shiloach Joseph Laboratory of Cellular and Developmental Biology, NIDDKD, 20895-0520, Bethesda, MD, U.S.A aut NATIONALLICENCE 700 1- Gronenborn Angela Laboratory of Chemical Physics, NIDDKD, National Institutes of Health, Building 5, 20892-0520, Bethesda, MD, U.S.A aut NATIONALLICENCE 773 0- Journal of Biomolecular NMR Kluwer Academic Publishers 10/4(1997-12-01), 317-328 0925-2738 10:4<317 1997 10 10858 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer