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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5
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pubmed:dateCreated |
1999-6-3
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pubmed:databankReference |
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pubmed:abstractText |
The 2.7 A X-ray crystal structure of the DNA-binding domain (DBD) of the orphan nuclear receptor, nerve growth factor-induced-B (NGFI-B), complexed to its high-affinity DNA target, represents the first structure analysis of a nuclear receptor DBD bound as a monomer to DNA. The structure of the core DBD and its interactions with the major groove of the DNA are similar to previously crystallographically solved DBD-DNA complexes in this superfamily; however, residues C-terminal to this core form a separate and unique substructure that interacts extensively and in a sequence-specific way with the minor groove of its DNA target, in particular with the characteristic 3 A-T base-pair identity element that extends 5' to the usual nuclear receptor half-site (AGGTCA).
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nr1d1 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Nr4a1 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Receptor Subfamily 1...,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Receptor Subfamily 4...,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cytoplasmic and Nuclear,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Steroid,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
1072-8368
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
6
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
471-7
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:10331876-Amino Acid Sequence,
pubmed-meshheading:10331876-Animals,
pubmed-meshheading:10331876-Base Sequence,
pubmed-meshheading:10331876-Binding Sites,
pubmed-meshheading:10331876-Crystallization,
pubmed-meshheading:10331876-Crystallography, X-Ray,
pubmed-meshheading:10331876-DNA,
pubmed-meshheading:10331876-DNA-Binding Proteins,
pubmed-meshheading:10331876-Hydrogen Bonding,
pubmed-meshheading:10331876-Models, Molecular,
pubmed-meshheading:10331876-Molecular Sequence Data,
pubmed-meshheading:10331876-Nuclear Receptor Subfamily 1, Group D, Member 1,
pubmed-meshheading:10331876-Nuclear Receptor Subfamily 4, Group A, Member 1,
pubmed-meshheading:10331876-Peptide Fragments,
pubmed-meshheading:10331876-Protein Binding,
pubmed-meshheading:10331876-Protein Conformation,
pubmed-meshheading:10331876-Proteins,
pubmed-meshheading:10331876-Rats,
pubmed-meshheading:10331876-Receptors, Cytoplasmic and Nuclear,
pubmed-meshheading:10331876-Receptors, Steroid,
pubmed-meshheading:10331876-Response Elements,
pubmed-meshheading:10331876-Thermodynamics,
pubmed-meshheading:10331876-Transcription Factors
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pubmed:year |
1999
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pubmed:articleTitle |
DNA-binding mechanism of the monomeric orphan nuclear receptor NGFI-B.
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pubmed:affiliation |
Department of Molecular Biophysics and Biochemistry and the Howard Hughes Medical Institute, Yale University, New Haven, Connecticut 06511, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.
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