1ZNF
THREE-DIMENSIONAL SOLUTION STRUCTURE OF A SINGLE ZINC FINGER DNA-BINDING DOMAIN
1ZNF の概要
エントリーDOI | 10.2210/pdb1znf/pdb |
分子名称 | 31ST ZINC FINGER FROM XFIN, ZINC ION (2 entities in total) |
機能のキーワード | zinc finger dna binding domain |
由来する生物種 | Xenopus laevis (African clawed frog) |
細胞内の位置 | Cytoplasm : P08045 |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 3073.92 |
構造登録者 | Lee, M.S.,Gippert, G.P.,Soman, K.V.,Case, D.A.,Wright, P.E. (登録日: 1989-09-25, 公開日: 1991-07-15, 最終更新日: 2017-11-29) |
主引用文献 | 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 Cited by 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主引用文献が同じPDBエントリー |
実験手法 | SOLUTION NMR |
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