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XB-ART-14319
J Biomol NMR 1998 Jul 01;121:51-71. doi: 10.1023/a:1008290631575.
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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.

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


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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.

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Species referenced: Xenopus laevis
Genes referenced: gtf3a

References [+] :
Berg, Zinc finger domains: hypotheses and current knowledge. 1990, Pubmed