3N00: Crystal Structure Of A Deletion Mutant Of Human Reverba Ligand Binding Domain Bound With An Ncor Id1 Peptide Determined To 2.60a

Repression of gene transcription by the nuclear receptor Rev-erbalpha plays an integral role in the core molecular circadian clock. We report the crystal structure of a nuclear receptor-co-repressor (N-CoR) interaction domain 1 (ID1) peptide bound to truncated human Rev-erbalpha ligand-binding domain (LBD). The ID1 peptide forms an unprecedented antiparallel beta-sheet with Rev-erbalpha, as well as an alpha-helix similar to that seen in nuclear receptor ID2 crystal structures but out of register by four residues. Comparison with the structure of Rev-erbbeta bound to heme indicates that ID1 peptide and heme induce substantially different conformational changes in the LBD. Although heme is involved in Rev-erb repression, the structure suggests that Rev-erbalpha could also mediate repression via ID1 binding in the absence of heme. The previously uncharacterized secondary structure induced by ID1 peptide binding advances our understanding of nuclear receptor-co-repressor interactions.
PDB ID: 3N00Download
MMDB ID: 83100
PDB Deposition Date: 2010/5/13
Updated in MMDB: 2017/08
Experimental Method:
x-ray diffraction
Resolution: 2.6  Å
Source Organism:
Similar Structures:
Biological Unit for 3N00: tetrameric; determined by author and by software (PISA)
Molecular Components in 3N00
Label Count Molecule
Proteins (4 molecules)
Rev-erba-alpha(Gene symbol: NR1D1)
Molecule annotation
Nuclear Receptor Corepressor 1(Gene symbol: NCOR1)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB