1CIT

DNA-BINDING MECHANISM OF THE MONOMERIC ORPHAN NUCLEAR RECEPTOR NGFI-B

Summary for 1CIT

• Entry DOI: 10.2210/pdb1cit/pdb
• Descriptor: DNA (5'-D(*CP*CP*GP*AP*AP*AP*AP*GP*GP*TP*CP*AP*TP*GP*CP*G)-3'), DNA (5'-D(*CP*GP*CP*AP*TP*GP*AP*CP*CP*TP*TP*TP*TP*CP*GP*G)-3'), PROTEIN (ORPHAN NUCLEAR RECEPTOR NGFI-B), ... (5 entities in total)
• Functional Keywords: orphan nuclear receptor, early immediate response gene product, transcription factor, monomeric protein-dna complex, minor groove interactions, protein/dna, transcription-dna complex, transcription/dna
• Biological source: Rattus norvegicus (Norway rat)
• Cellular location: Nucleus: P22829
• Total number of polymer chains: 3
• Total formula weight: 20027.15

Authors

Meinke, G.,Sigler, P.B. (deposition date: 1999-04-05, release date: 1999-05-03, Last modification date: 2023-08-09)

Primary citation

Meinke, G.,Sigler, P.B.
DNA-binding mechanism of the monomeric orphan nuclear receptor NGFI-B.
Nat.Struct.Biol., 6:471-477, 1999

PubMed Abstract: 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).

PubMed: 10331876
DOI: 10.1038/8276

Experimental method

X-RAY DIFFRACTION (2.7 Å)