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 backbone 1HN, 15N, 13Cα and 13Cβ 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.
Original language | English (US) |
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Pages (from-to) | 51-71 |
Number of pages | 21 |
Journal | Journal of Biomolecular NMR |
Volume | 12 |
Issue number | 1 |
DOIs | |
State | Published - 1998 |
Funding
The authors acknowledge J. Cavanagh and M. Rance for assistance with NMR experiments, L. Xiang and G.P. Gippert for semiautomated NMR assignment tools, D. Case for implementation of ambiguous restraints in AMBER, J. Love, D. Casimiro, D. Sem, S. Holmbeck and J. Dyson for helpful discussions, and Tripos Inc. and MSI Inc. for providing NMR processing and analysis software. M.P.F. was supported by a postdoctoral fellowship from the American Cancer Society, D.S.W. by an NSF postdoctoral fellowship, I.R. by a fellowship from the Jane Coffin Childs Research Foundation, and W.J. by a Studienstiftung des Deutschen Volkes. This work was supported by Grant GM36643 from the National Institutes of Health.
Keywords
- Binding
- Chemical shift
- Complex
- DNA
- Structure
- TFIIIA
- Zinc Finger
ASJC Scopus subject areas
- Biochemistry
- Spectroscopy