1HRA

THE SOLUTION STRUCTURE OF THE HUMAN RETINOIC ACID RECEPTOR-BETA DNA-BINDING DOMAIN

1HRA の概要

• エントリーDOI: 10.2210/pdb1hra/pdb
• 分子名称: RETINOIC ACID RECEPTOR, ZINC ION (2 entities in total)
• 機能のキーワード: dna-binding receptor
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Isoform Beta-1: Nucleus. Isoform Beta-2: Nucleus. Isoform Beta-4: Cytoplasm: P10826
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9564.89

構造登録者

Knegtel, R.M.A.,Katahira, M.,Schilthuis, J.G.,Bonvin, A.M.J.J.,Boelens, R.,Eib, D.,Van Der Saag, P.T.,Kaptein, R. (登録日: 1993-07-25, 公開日: 1994-01-31, 最終更新日: 2024-05-22)

主引用文献

Knegtel, R.M.,Katahira, M.,Schilthuis, J.G.,Bonvin, A.M.,Boelens, R.,Eib, D.,van der Saag, P.T.,Kaptein, R.
The solution structure of the human retinoic acid receptor-beta DNA-binding domain.
J.Biomol.NMR, 3:1-17, 1993

PubMed Abstract: The three-dimensional structure of the DNA-binding domain of the human retinoic acid receptor-beta (hRAR-beta) has been determined by nuclear magnetic resonance spectroscopy in conjunction with distance geometry, restrained molecular dynamics and iterative relaxation matrix calculations. A total of 1244 distance restraints were obtained from NOE intensities, of which 448 were intra-residue and 796 inter-residue restraints. In addition 23 chi and 30 phi dihedral angle restraints were obtained from J-coupling data. The two 'zinc-finger' regions of the 80-amino acid residue protein are followed by two alpha-helices that cross each other perpendicularly. There is a short stretch of b-sheet near the N-terminus. The alpha-helical core of the protein is well determined with a backbone root-mean-square deviation (r.m.s.d.) with respect to the average of 0.18 A and 0.37 A when the side chains of residues 31, 32, 36, 61, 62, 65 and 69 are included. The r.m.s.d. for the backbone of residues 5-80 is 0.76 A. For the first finger (residues 8-28), the r.m.s.d. of the backbone is 0.79 A. For the second finger (residues 44-62) the r.m.s.d. is 0.64 A. The overall structure is similar to that of the corresponding domain of the glucocorticoid receptor, although the C-terminal part of the protein is different. The second alpha-helix is two residues shorter and is followed by a well-defined region of extended backbone structure.

PubMed: 8383553
DOI: 10.1007/BF00242472

実験手法

SOLUTION NMR