1HRA
THE SOLUTION STRUCTURE OF THE HUMAN RETINOIC ACID RECEPTOR-BETA DNA-BINDING DOMAIN
Summary for 1HRA
| Entry DOI | 10.2210/pdb1hra/pdb |
| Descriptor | RETINOIC ACID RECEPTOR, ZINC ION (2 entities in total) |
| Functional Keywords | dna-binding receptor |
| Biological source | Homo sapiens (human) |
| Cellular location | Isoform Beta-1: Nucleus. Isoform Beta-2: Nucleus. Isoform Beta-4: Cytoplasm: P10826 |
| Total number of polymer chains | 1 |
| Total formula weight | 9564.89 |
| Authors | 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. (deposition date: 1993-07-25, release date: 1994-01-31, Last modification date: 2024-05-22) |
| Primary citation | 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 Cited by 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: 8383553DOI: 10.1007/BF00242472 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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