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. Journal Article uri icon



  • 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 backbone 1HN, 15N, 13C alpha and 13C beta 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.

publication date

  • July 1, 1998

has subject area

has restriction

  • closed

Date in CU Experts

  • October 1, 2013 12:30 PM

Full Author List

  • Foster MP; Wuttke DS; Clemens KR; Jahnke W; Radhakrishnan I; Tennant L; Reymond M; Chung J; Wright PE

author count

  • 9

Other Profiles

International Standard Serial Number (ISSN)

  • 0925-2738

Additional Document Info

start page

  • 51

end page

  • 71


  • 12


  • 1