Summary information and primary citation
- PDB-id
-
1cit;
DSSR-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).
