1hra: Difference between revisions

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[[Image:1hra.gif|left|200px]]
{{Seed}}
[[Image:1hra.png|left|200px]]


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{{STRUCTURE_1hra|  PDB=1hra  |  SCENE=  }}  
{{STRUCTURE_1hra|  PDB=1hra  |  SCENE=  }}  


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




==Overview==
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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.
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{{ABSTRACT_PUBMED_8383553}}


==About this Structure==
==About this Structure==
1HRA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HRA OCA].  
1HRA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HRA OCA].  


==Reference==
==Reference==
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[[Category: Schilthuis, J G.]]
[[Category: Schilthuis, J G.]]
[[Category: Dna-binding receptor]]
[[Category: Dna-binding receptor]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:09:17 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:34:41 2008''

Revision as of 05:34, 1 July 2008

File:1hra.png

Template:STRUCTURE 1hra

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

Template:ABSTRACT PUBMED 8383553

About this Structure

1HRA is a Single protein structure of sequence from Homo sapiens. Full experimental 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

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