Structural role of a detergent molecule in retinoic acid nuclear receptor crystals

• Published in: Acta crystallographica. Section D, Biological crystallography. Vol. 56; no. 7; pp. 933 - 935
• Main Authors: Klaholz, Bruno P., Moras, Dino
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England Munksgaard International Publishers 01.07.2000
• Subjects: Crystallization; detergents; Detergents - chemistry; Humans; Models, Molecular; Protein Conformation; Receptors, Retinoic Acid - chemistry; retinoic acid nuclear receptor; Retinoic Acid Receptor gamma
• ISSN: 1399-0047; 0907-4449; 1399-0047
• DOI: 10.1107/S090744490000634X

The human nuclear receptor of retinoic acid hRARγ is a ligand‐dependent transcription regulator. The presence of a completely ordered dodecyl‐α‐d‐maltoside molecule in the crystal structure of the hRARγ ligand‐binding domain (LBD) refined at 1.3 Å resolution is reported. The non‐ionic detergent is required for stabilization and crystallization of the hRARγ 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.