Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
|
| pubmed:dateCreated |
1993-4-13
|
| pubmed:abstractText |
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:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Deoxyribonuclease I,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Retinoic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tretinoin
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jan
|
| pubmed:issn |
0925-2738
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
3
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
1-17
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:8383553-Amino Acid Sequence,
pubmed-meshheading:8383553-Base Sequence,
pubmed-meshheading:8383553-Binding Sites,
pubmed-meshheading:8383553-Carrier Proteins,
pubmed-meshheading:8383553-Cloning, Molecular,
pubmed-meshheading:8383553-DNA,
pubmed-meshheading:8383553-DNA-Binding Proteins,
pubmed-meshheading:8383553-Deoxyribonuclease I,
pubmed-meshheading:8383553-Humans,
pubmed-meshheading:8383553-Magnetic Resonance Spectroscopy,
pubmed-meshheading:8383553-Models, Molecular,
pubmed-meshheading:8383553-Molecular Sequence Data,
pubmed-meshheading:8383553-Protein Structure, Secondary,
pubmed-meshheading:8383553-Receptors, Retinoic Acid,
pubmed-meshheading:8383553-Recombinant Proteins,
pubmed-meshheading:8383553-Restriction Mapping,
pubmed-meshheading:8383553-Tretinoin,
pubmed-meshheading:8383553-Zinc Fingers
|
| pubmed:year |
1993
|
| pubmed:articleTitle |
The solution structure of the human retinoic acid receptor-beta DNA-binding domain.
|
| pubmed:affiliation |
Department of Chemistry, University of Utrecht, The Netherlands.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|