1rjk Summary

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crystal structure of the rat vitamin D receptor ligand binding domain complexed with 2MD and a synthetic peptide containing the NR2 box of DRIP 205

The structure was published by Vanhooke, J.L., Benning, M.M., Bauer, C.B., Pike, J.W., and DeLuca, H.F., in 2004 in a paper entitled "Molecular Structure of the Rat Vitamin D Receptor Ligand Binding Domain Complexed with 2-Carbon-Substituted Vitamin D(3) Hormone Analogues and a LXXLL-Containing Coactivator Peptide" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.99 Å and deposited in 2003.

The experimental data on which the structure is based was also deposited.

This PDB entry contains a complex of 2 biomacromolecules, namely Vitamin D3 receptor and Peroxisome proliferator-activated receptor binding protein.

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):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A Vitamin D3 receptor P13053 (116-423) (VDR_RAT)search Rattus norvegicussearch < 90% 292 81%
C Peroxisome proliferator-activated receptor binding protein Q15648 (640-652) (MED1_HUMAN)search Homo sapienssearch < 90% 13 84%


This entry contains 2 unique UniProt proteins:

UniProt accession Name Organism PDB
P13053 (116 - 423) Vitamin D3 receptor Rattus norvegicus
Q15648 (640 - 652) Peroxisome proliferator-activated receptor binding protein

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A Nuclear receptor ligand-binding domainsearch Retinoid X Receptorsearch Ligand-binding domain of nuclear hormone receptorsearch
C

Chain ID Molecular function (GO) Cellular component (GO) Biological process (GO)
A (P13053) steroid hormone receptor activitysearch sequence-specific DNA binding transcription factor activitysearch DNA bindingsearch thyroid hormone receptor activitysearch nucleussearch regulation of transcription, DNA-templatedsearch steroid hormone mediated signaling pathwaysearch

Chain InterPro annotation
A Nuclear hormone receptor, ligand-binding, coresearch Steroid hormone receptorsearch Thyroid hormone receptorsearch Nuclear hormone receptor, ligand-bindingsearch
C