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1hra
From Proteopedia
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THE SOLUTION STRUCTURE OF THE HUMAN RETINOIC ACID RECEPTOR-BETA DNA-BINDING DOMAIN
Contents |
Overview
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.
Disease
Known disease associated with this structure: Camptodactyly-arthropathy-coxa vara-pericarditis syndrome OMIM:[604283]
About this Structure
1HRA is a Single protein structure of sequence from Homo sapiens with ZN as ligand. Full crystallographic information is available from OCA.
Reference
The solution structure of the human retinoic acid receptor-beta DNA-binding domain., Knegtel RM, Katahira M, Schilthuis JG, Bonvin AM, Boelens R, Eib D, van der Saag PT, Kaptein R, J Biomol NMR. 1993 Jan;3(1):1-17. PMID:8383553
Page seeded by OCA on Mon Nov 12 17:21:20 2007
