DNA-binding mechanism of the monomeric orphan nuclear receptor NGFI-B

Citation
G. Meinke et Pb. Sigler, DNA-binding mechanism of the monomeric orphan nuclear receptor NGFI-B, NAT ST BIOL, 6(5), 1999, pp. 471-477
Citations number
45
Categorie Soggetti
Biochemistry & Biophysics
Journal title
NATURE STRUCTURAL BIOLOGY
ISSN journal
10728368 → ACNP
Volume
6
Issue
5
Year of publication
1999
Pages
471 - 477
Database
ISI
SICI code
1072-8368(199905)6:5<471:DMOTMO>2.0.ZU;2-R
Abstract
The 2.7 Angstrom X-ray crystal structure of the DNA-binding domain (DBD) of the orphan nuclear receptor, nerve growth factor-induced-B (NGFI-B), compl exed to its high-affinity DNA target, represents the first structure analys is of a nuclear receptor DBD bound as a monomer to DNA. The structure of th e core DBD and its interactions with the major groove of the DNA are simila r to previously crystallographically solved DBD-DNA complexes in this super family; however, residues C-terminal to this core form a separate and uniqu e substructure that interacts extensively and in a sequence-specific way wi th the minor groove of its DNA target, in particular with the characteristi c 3 A-T base-pair identity element that extends 5' to the usual nuclear rec eptor half-site (AGGTCA).