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

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 r...

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Bibliographic Details
Published in:Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2000-07, Vol.56 (7), p.933-935
Main Authors: Klaholz, Bruno P., Moras, Dino
Format: Article
Language:English
Subjects:
Crystallization
detergents
Detergents - chemistry
Humans
Models, Molecular
Protein Conformation
Receptors, Retinoic Acid - chemistry
retinoic acid nuclear receptor
Retinoic Acid Receptor gamma
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Summary: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.
ISSN:1399-0047
0907-4449
1399-0047
DOI:10.1107/S090744490000634X