1ZNF

THREE-DIMENSIONAL SOLUTION STRUCTURE OF A SINGLE ZINC FINGER DNA-BINDING DOMAIN

Summary for 1ZNF

• Entry DOI: 10.2210/pdb1znf/pdb
• Descriptor: 31ST ZINC FINGER FROM XFIN, ZINC ION (2 entities in total)
• Functional Keywords: zinc finger dna binding domain
• Biological source: Xenopus laevis (African clawed frog)
• Cellular location: Cytoplasm : P08045
• Total number of polymer chains: 1
• Total formula weight: 3073.92

Authors

Lee, M.S.,Gippert, G.P.,Soman, K.V.,Case, D.A.,Wright, P.E. (deposition date: 1989-09-25, release date: 1991-07-15, Last modification date: 2024-11-20)

Primary citation

Lee, M.S.,Gippert, G.P.,Soman, K.V.,Case, D.A.,Wright, P.E.
Three-dimensional solution structure of a single zinc finger DNA-binding domain.
Science, 245:635-637, 1989

PubMed 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.

PubMed: 2503871

Experimental method

SOLUTION NMR