Structural role of a detergent molecule in retinoic acid nuclear receptor crystals.
The human nuclear receptor of retinoic acid hRARgamma is a ligand-dependent transcription regulator. The presence of a completely ordered dodecyl-alpha-D-maltoside molecule in the crystal structure of the hRARgamma ligand-binding domain (LBD) refined at 1. 3 A resolution is reported. The non-ionic detergent is required for stabilization and crystallization of the hRARgamma LBD and mediates a crystal contact in the region where coactivator proteins bind. Its dodecyl moiety is buried in a hydrophobic channel, whereas the maltoside head group is hydrogen bonded to water molecules and polar residue side chains.
Klaholz
B P
BP
Laboratoire de Biologie Structurale, Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS/INSERM/ULP, 1 Rue Laurent Fries, BP 163, F-67404 Illkirch CEDEX, France.
Moras
D
D
D003460:Crystallization; D003902:Detergents / Q000737:chemistry*; D006801:Humans; D008958:Models, Molecular; D011487:Protein Conformation; D018168:Receptors, Retinoic Acid / Q000737:chemistry*; D000097768:Retinoic Acid Receptor gamma
D003902:Detergents; D018168:Receptors, Retinoic Acid; D000097768:Retinoic Acid Receptor gamma