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Three-Dimensional Solution Structure of a Single Zinc Finger DNA-Binding Domain

Lee, Min S., Gippert, Garry P., Soman, Kizhake V., Case, David A., Wright, Peter E.·1989·Science

Abstract

The three-dimensional solution structure of a zinc finger nucleic acid binding motif has been determined by nuclear magnetic resonance (NMR) spectroscopy. Spectra of a synthetic peptide corresponding to a single zinc finger from the Xenopus protein Xfin yielded distance and dihedral angle constraints that were used to generate structures from distance geometry and restrained molecular dynamics calculations. The zinc finger is an independently folded domain with a compact globular structure in which the zinc atom is bound by two cysteine and two histidine ligands. The polypeptide backbone fold consists of a well-defined helix, starting as alpha and ending as 3(10) helix, packed against two beta strands that are arranged in a hairpin structure. A high density of basic and polar amino acid side chains on the exposed face of the helix are probably involved in DNA binding.

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Metadata

Authors
Lee, M. S., Gippert, G. P., Soman, K. V., Case, D. A., & Wright, P. E.
Venue
Science
Published
1989-08-11
Volume
245
Issue
4918
Pages
635-637
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2030333654
Cited by
627
References
0
FWCI
21.08
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Three-Dimensional Solution Structure of a Single Zinc Finger DNA-Binding Domain. https://app.cochat.ai/papers/10.1126/science.2503871
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Lee, M. S., Gippert, G. P., Soman, K. V., Case, D. A., & Wright, P. E. (1989). Three-Dimensional Solution Structure of a Single Zinc Finger DNA-Binding Domain. Science. https://doi.org/10.1126/science.2503871

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.