CAR: three new models for a problem child

David D Moore

doi:10.1016/j.cmet.2004.12.006

CAR: three new models for a problem child

Cell Metab. 2005 Jan;1(1):6-8. doi: 10.1016/j.cmet.2004.12.006.

Author

David D Moore¹

Affiliation

¹ Department of Molecular and Cellular Biology, Baylor College of Medicine, Houston, Texas 77030, USA.

PMID: 16054039
DOI: 10.1016/j.cmet.2004.12.006

Abstract

By comparison with its older and better-behaved cousins in the nuclear receptor superfamily, CAR (NR1I3) has always been an oddball. Three new crystal structures recently described in Molecular Cell reveal the molecular basis for some of its bad habits (Xu et al., 2004; Suino et al., 2004; Shan et al., 2004).

MeSH terms

Amino Acid Motifs
Animals
Constitutive Androstane Receptor
Humans
Ligands
Protein Binding
Protein Conformation
Receptors, Cytoplasmic and Nuclear / chemistry*
Receptors, Cytoplasmic and Nuclear / physiology*
Transcription Factors / chemistry*
Transcription Factors / physiology*
Transcriptional Activation

Substances

Constitutive Androstane Receptor
Ligands
NR1I3 protein, human
Receptors, Cytoplasmic and Nuclear
Transcription Factors