TR Receptor Mutations Conferring Hormone Resistance and Reduced Corepressor Release Exhibit Decreased Stability in the Nterminal LBD
The structure was published by Huber, B.R., Desclozeaux, M., West, B.L., et al., Baxter, J.D., Ingraham, H.A., and Fletterick, R.J., in 2003 in a paper entitled "Thyroid hormone receptor-beta mutations conferring hormone resistance and reduced corepressor release exhibit decreased stability in the N-terminal ligand-binding domain" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.4 Å and deposited in 2003.
The experimental data on which the structure is based was not deposited.
The PDB entry contains the structure of Thyroid hormone receptor beta-1. This molecule has the UniProt identifier P10828 (THB_HUMAN). The sample contained 263 residues which is < 90% of the natural sequence. Out of 263 residues 249 were observed and are deposited in the PDB.
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 has more than one probable quaternary state observed. For more details see the quaternary structure page.
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: