Bibliographic Details
| Title: |
Structure of Rev-erbα bound to N-CoR reveals a unique mechanism of nuclear receptor–co-repressor interaction. |
| Authors: |
Phelan, Caroline A.1, Gampe, Robert T.2, Lambert, Millard H.2, Parks, Derek J.3, Montana, Valerie2, Bynum, Jane3, Broderick, Timothy M.3, Xiao Hu1, Williams, Shawn P.2, Nolte, Robert T.2 robert.t.nolte@gsk.com, Lazar, Mitchell A.1 lazar@mail.med.upenn.edu |
| Source: |
Nature Structural & Molecular Biology. Jul2010, Vol. 17 Issue 7, p808-814. 7p. 4 Diagrams, 1 Chart, 1 Graph. |
| Subject Terms: |
*GENETIC transcription, *NUCLEAR receptors (Biochemistry), *CIRCADIAN rhythms, *HEMOPROTEINS, *LEWY body dementia |
| Abstract: |
Repression of gene transcription by the nuclear receptor Rev-erbα 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-erbα ligand-binding domain (LBD). The ID1 peptide forms an unprecedented antiparallel β-sheet with Rev-erbα, as well as an α-helix similar to that seen in nuclear receptor ID2 crystal structures but out of register by four residues. Comparison with the structure of Rev-erbβ 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-erbα 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. [ABSTRACT FROM AUTHOR] |
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| Database: |
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