Crystal structure of the RAR-γ ligand-binding domain bound to all-trans retinoic acid
Open Access
- 14 December 1995
- journal article
- research article
- Published by Springer Nature in Nature
- Vol. 378 (6558) , 681-689
- https://doi.org/10.1038/378681a0
Abstract
The 2.0-Å crystal structure of the ligand-binding domain (LBD) of the human retinoic acid receptor (RAR)-γ bound to all-trans retinoic acid reveals the ligand-binding interactions and suggests an electrostatic guidance mechanism. The overall fold is similar to that of the human RXR-α apo-LBD, except for the carboxy-terminal part which folds back towards the LBD core, contributing to the hydrophobic ligand pocket and 'sealing' its entry site. We propose a 'mouse trap' mechanism whereby a ligand-induced conformational transition repositions the amphi-pathic α-helix of the AF-2 activating domain and forms a transcriptionally active receptor.Keywords
This publication has 49 references indexed in Scilit:
- Multiplicity generates diversity in the retinoic acid signalling pathwaysPublished by Elsevier ,2003
- Structural determinants of nuclear receptor assembly on DNA direct repeatsNature, 1995
- How to finger DNANature, 1995
- Interaction of thyroid-hormone receptor with a conserved transcriptional mediatorNature, 1995
- Interaction of proteins with transcriptionally active estrogen receptors.Proceedings of the National Academy of Sciences, 1994
- Estrogen Receptor-Associated Proteins: Possible Mediators of Hormone-Induced TranscriptionScience, 1994
- The retinoid signaling pathway: molecular and genetic analysesSeminars in Cell Biology, 1994
- The crystal structure of the estrogen receptor DNA-binding domain bound to DNA: How receptors discriminate between their response elementsCell, 1993
- Crystallographic analysis of the interaction of the glucocorticoid receptor with DNANature, 1991
- v-erbA oncogene activation entails the loss of hormone-dependent regulator activity of c-erbACell, 1990