First time at Proteopedia? Click on the green links: they change the 3D image. Click and drag the molecules. Proteopedia is a 3D, interactive encyclopedia of proteins, RNA, DNA and other molecules. With a free user account, you can edit pages in Proteopedia. Visit the Main Page to learn more.

1dkf

From Proteopedia

Jump to: navigation, search

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

1dkf, resolution 2.50Å ()

Ligands:

Domains:

Hormone_recep

Related:

1lbd, 2lbd

Structural annotation:
Resources:	CATH : 1Dkfa00, 1Dkfb00 InterPro : Ipr000536, Ipr001723, Ipr001628, Ipr008946, Ipr000003, Ipr003078 Pfam : PF00104 SCOP : d1dkfa_, d1dkfb_ UniProt : P28700, P10276

Functional annotation:
Resources:	GeneCard : RARA
Cellular component:	nucleus
Biological process:	cardiac muscle cell proliferation transcription ventricular cardiac muscle cell differentiation positive regulation of transcription from RNA polymerase II promoter regulation of transcription, DNA-dependent ventricular cardiac muscle morphogenesis heart development signal transduction
Molecular function:	transcription factor activity DNA binding protein binding ligand-dependent nuclear receptor activity zinc ion binding metal ion binding steroid binding tRNA-pseudouridine synthase activity transcription regulator activity steroid hormone receptor activity receptor activity sequence-specific DNA binding transcription coactivator activity retinoic acid receptor activity

Evolutionary conservation:

Toggle Conservation Colors:

Rows = identical sequences:

Further Information:

Caveats,

Explanation,
Complete Results at ConSurfDB

Resources:

FirstGlance, OCA, PDBsum, RCSB

Coordinates:

save as pdb, mmCIF, xml

CRYSTAL STRUCTURE OF A HETERODIMERIC COMPLEX OF RAR AND RXR LIGAND-BINDING DOMAINS

Publication Abstract from PubMed

The crystal structure of a heterodimer between the ligand-binding domains (LBDs) of the human RARalpha bound to a selective antagonist and the constitutively active mouse RXRalphaF318A mutant shows that, pushed by a bulky extension of the ligand, RARalpha helix H12 adopts an antagonist position. The unexpected presence of a fatty acid in the ligand-binding pocket of RXRalpha(F318A is likely to account for its apparent "constitutivity." Specific conformational changes suggest the structural basis of pure and partial antagonism. The RAR-RXR heterodimer interface is similar to that observed in most nuclear receptor (NR) homodimers. A correlative analysis of 3D structures and sequences provides a novel view on dimerization among members of the nuclear receptor superfamily.

Crystal structure of a heterodimeric complex of RAR and RXR ligand-binding domains., Bourguet W, Vivat V, Wurtz JM, Chambon P, Gronemeyer H, Moras D, Mol Cell. 2000 Feb;5(2):289-98. PMID:10882070

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

1DKF is a 2 chains structure of sequences from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA.

Reference

Bourguet W, Vivat V, Wurtz JM, Chambon P, Gronemeyer H, Moras D. Crystal structure of a heterodimeric complex of RAR and RXR ligand-binding domains. Mol Cell. 2000 Feb;5(2):289-98. PMID:10882070

Page seeded by OCA on Mon Feb 16 12:41:54 2009

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://www.proteopedia.org/wiki/index.php/1dkf"

1dkf

From Proteopedia

CRYSTAL STRUCTURE OF A HETERODIMERIC COMPLEX OF RAR AND RXR LIGAND-BINDING DOMAINS

About this Structure

Reference

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

random

Search

Toolbox