Article
Identification of a novel co-regulator interaction surface on the ligand binding domain of Nurr1 using NMR footprinting.
The Journal of biological chemistry - 17 Dec 2004
Codina Anna, Benoit Gerard, Gooch John T, Neuhaus David, Perlmann Thomas, Schwabe John W R
Abstract excerpt
The nuclear receptor Nurr1 is a transcription factor essential for the development of midbrain dopaminergic neurons in vertebrates. Recent crystal structures of the Nurr1 ligand binding domain (LBD) and the Drosophila orthologue dHR38 revealed that, although these receptors share the classical LBD architecture, they lack a ligand binding cavity. This volume is instead filled with bulky hydrophobic side chains....
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.
