Three-dimensional solution structure of a single zinc finger DNA-binding domain

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

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    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 α and ending as 3 10 helix, packed against two β 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.

    Original languageEnglish (US)
    Pages (from-to)635-637
    Number of pages3
    JournalScience
    Volume245
    Issue number4918
    DOIs
    StatePublished - Jan 1 1989

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    ASJC Scopus subject areas

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    Cite this

    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, 245(4918), 635-637. https://doi.org/10.1126/science.2503871