ISDA: 1CIT

Deposition Date 1999-04-05

Release Date 1999-05-03

Last Version Date 2023-08-09

Entry Detail

PDB ID:

1CIT

Keywords:

TRANSCRIPTION/DNA

Title:

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

Biological Source:

Source Organism(s):

Rattus norvegicus (Taxon ID: 10116)

Expression System(s):

Escherichia coli bl21(de3)

Method Details:

Experimental Method:

X-RAY DIFFRACTION

Resolution:

2.70 Å

R-Value Free:

0.29

R-Value Work:

0.21

Space Group:

P 1 21 1

Download Validation Report

Macromolecular Entities

Structures with similar UniProt ID

Structural Superimposition Protein Blast

Polymer Type:polypeptide(L)
Molecule:PROTEIN (ORPHAN NUCLEAR RECEP
Gene (Uniprot):Nr4a1
Chain IDs:C (auth: A)
Chain Length:89
Number of Molecules:1
Biological Source:Rattus norvegicus

UniProt ID:P22829 Pfam ID:PF00105

Ligand Molecules

Primary Citation

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

Meinke, G, Sigler, P.B.Show

Nat. Struct. Biol. 6 471 477 (1999)

PMID: 10331876 DOI: 10.1038/8276

Abstact

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).

Legend

Protein

Chemical

Disease

Primary Citation of related structures

Abstact

Feedback Form