Summary information and primary citation
- PDB-id
- 1cit; SNAP-derived features in text and JSON formats;
DNAproDB
- Class
- transcription-DNA
- Method
- X-ray (2.7 Å)
- Summary
- DNA-binding mechanism of the monomeric orphan nuclear receptor ngfi-b
- Reference
- Meinke G, Sigler PB (1999): "DNA-binding mechanism of the monomeric orphan nuclear receptor NGFI-B." Nat.Struct.Biol., 6, 471-477. doi: 10.1038/8276.
- 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).
