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

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.

[1]  M. Karplus,et al.  Crystallographic refinement by simulated annealing: application to crambin , 1989 .

[2]  L. Hood,et al.  Zinc-dependent structure of a single-finger domain of yeast ADR1. , 1988, Science.

[3]  P Argos,et al.  A model for the tertiary structure of the 28 residue DNA-binding motif ('zinc finger') common to many eukaryotic transcriptional regulatory proteins. , 1988, Protein engineering.

[4]  K. Yamamoto,et al.  The function and structure of the metal coordination sites within the glucocorticoid receptor DNA binding domain , 1988, Nature.

[5]  A. Vincent,et al.  Finger proteins and DNA‐specific recognition: Distinct patterns of conserved amino acids suggest different evolutionary modes , 1988, FEBS letters.

[6]  K. Nasmyth,et al.  Zinc-finger motifs expressed in E. coli and folded in vitro direct specific binding to DNA , 1988, Nature.

[7]  H. Jäckle,et al.  Disruption of a putative Cys–zinc interaction eliminates the biological activity of the Krüppel finger protein , 1988, Nature.

[8]  R. Evans,et al.  Zinc fingers: Gilt by association , 1988, Cell.

[9]  J. Berg,et al.  Proposed structure for the zinc-binding domains from transcription factor IIIA and related proteins. , 1988, Proceedings of the National Academy of Sciences of the United States of America.

[10]  J. Berg,et al.  Metal-dependent folding of a single zinc finger from transcription factor IIIA. , 1987, Proceedings of the National Academy of Sciences of the United States of America.

[11]  Aaron Klug,et al.  ‘Zinc fingers’: a novel protein motif for nucleic acid recognition , 1987 .

[12]  A. Eisen,et al.  Two zinc fingers of a yeast regulatory protein shown by genetic evidence to be essential for its function , 1987, Nature.

[13]  A. Klug,et al.  EXAFS study of the zinc-binding sites in the protein transcription factor IIIA , 1986, Nature.

[14]  A. Klug,et al.  Mapping of the sites of protection on a 5 S RNA gene by the Xenopus transcription factor IIIA. A model for the interaction. , 1986, Journal of molecular biology.

[15]  P. Argos,et al.  Fingers and helices , 1986, Nature.

[16]  P. Kollman,et al.  An all atom force field for simulations of proteins and nucleic acids , 1986, Journal of computational chemistry.

[17]  Timothy F. Havel,et al.  Solution conformation of proteinase inhibitor IIA from bull seminal plasma by 1H nuclear magnetic resonance and distance geometry. , 1985, Journal of molecular biology.

[18]  H. Berendsen,et al.  Molecular dynamics with coupling to an external bath , 1984 .

[19]  K Wüthrich,et al.  Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-proton distance constraints with nuclear magnetic resonance. , 1983, Journal of molecular biology.

[20]  Richard R. Ernst,et al.  Investigation of exchange processes by two‐dimensional NMR spectroscopy , 1979 .