3N00

Crystal Structure of a deletion mutant of human Reverba ligand binding domain bound with an NCoR ID1 peptide determined to 2.60A

Summary for 3N00

• Entry DOI: 10.2210/pdb3n00/pdb
• Related: 2vov 3cqv
• Descriptor: Rev-erbA-alpha, Nuclear receptor corepressor 1 (3 entities in total)
• Functional Keywords: reverba ncorid1, anti-parallel b-sheet, transcription regulator
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: P20393 O75376
• Total number of polymer chains: 2
• Total formula weight: 30082.32

Authors

Gampe, R.,Nolte, R. (deposition date: 2010-05-13, release date: 2010-06-30, Last modification date: 2023-09-06)

Primary citation

Phelan, C.A.,Gampe, R.T.,Lambert, M.H.,Parks, D.J.,Montana, V.,Bynum, J.,Broderick, T.M.,Hu, X.,Williams, S.P.,Nolte, R.T.,Lazar, M.A.
Structure of Rev-erbalpha bound to N-CoR reveals a unique mechanism of nuclear receptor-co-repressor interaction.
Nat.Struct.Mol.Biol., 17:808-814, 2010

PubMed Abstract: 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.

PubMed: 20581824
DOI: 10.1038/nsmb.1860

Experimental method

X-RAY DIFFRACTION (2.6 Å)