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Chemical shift as a probe of molecular interfaces: NMR studies of DNA binding by the three amino-terminal zinc finger domains from transcription factor IIIA

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Abstract

We report the NMR resonance assignments for a macromolecular protein/DNA complex containing the three amino-terminal zinc fingers (92 amino acid residues) of Xenopus laevis TFIIIA (termed zf1-3) bound to the physiological DNA target (15 base pairs), and for the free DNA. Comparisons are made of the chemical shifts of protein backbone1 HN, 15N,13 Cα and13 Cβ and DNA base and sugar protons of the free and bound species. Chemical shift changes are analyzed in the context of the structures of the zf1-3/DNA complex to assess the utility of chemical shift change as a probe of molecular interfaces. Chemical shift perturbations that occur upon binding in the zf1-3/DNA complex do not correspond directly to the structural interface, but rather arise from a number of direct and indirect structural and dynamic effects.

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Authors and Affiliations

  1. Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA, 92037, U.S.A

    Mark P. Foster, Deborah S. Wuttke, Karen R. Clemens, Wolfgang Jahnke, Ishwar Radhakrishnan, Linda Tennant, Martine Reymond, John Chung & Peter E. Wright

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  1. Mark P. Foster
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  2. Deborah S. Wuttke
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  3. Karen R. Clemens
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  4. Wolfgang Jahnke
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Foster, M.P., Wuttke, D.S., Clemens, K.R. et al. Chemical shift as a probe of molecular interfaces: NMR studies of DNA binding by the three amino-terminal zinc finger domains from transcription factor IIIA. J Biomol NMR 12, 51–71 (1998). https://doi.org/10.1023/A:1008290631575

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