X-ray structure of benzisoxazole urea synthetic agonist bound to the LXR-alpha
The structure was published by Fradera, X., Vu, D., Nimz, O., et al., Bennett, D.J., McGuire, R., and Uitdehaag, J.C., in 2010 in a paper entitled "X-ray structures of the LXRalpha LBD in its homodimeric form and implications for heterodimer signaling." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.4 Å and deposited in 2009.
The experimental data on which the structure is based was also deposited.
This PDB entry contains a complex of 2 biomacromolecules, namely Oxysterols receptor LXR-alpha and Nuclear receptor coactivator 1.
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 heterotetramers.
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 2 unique UniProt proteins: