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.
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.
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BP
Klaholz
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Moras
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