THE 2.0 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF THE RXRALPHA LIGAND BINDING DOMAIN TETRAMER IN THE PRESENCE OF A NON-ACTIVATING RETINOIC ACID ISOMER.
The structure was published by Gampe Jr., R.T., Montana, V.G., Lambert, M.H., Wisely, G.B., Milburn, M.V., and Xu, H.E., in 2000 in a paper entitled "Structural basis for autorepression of retinoid X receptor by tetramer formation and the AF-2 helix." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 2000.
The experimental data on which the structure is based was not deposited.
This PDB entry contains multiple copies of the structure of RETINOIC ACID RECEPTOR RXR-ALPHA.
It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.
The molecule most likely forms homotetramers.
The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):
This entry contains 1 unique UniProt protein: