Communication between the ERRα Homodimer Interface and the PGC-1α Binding Surface via the Helix 8–9 Loop *
Journal of Biological Chemistry, ISSN: 0021-9258, Vol: 283, Issue: 29, Page: 20220-20230
2008
- 31Citations
- 39Captures
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Metrics Details
- Citations31
- Citation Indexes31
- 31
- CrossRef28
- Captures39
- Readers39
- 39
Article Description
Although structural studies on the ligand-binding domain (LBD) have established the general mode of nuclear receptor (NR)/coactivator interaction, determinants of binding specificity are only partially understood. The LBD of estrogen receptor-α (ERα), for example, interacts only with a region of peroxisome proliferator-activated receptor coactivator (PGC)-1α, which contains the canonical L XX LL motif (NR box2), whereas the LBD of estrogen-related receptor-α (ERRα) also binds efficiently an untypical, L XX YL-containing region (NR box3) of PGC-1α. Surprisingly, in a previous structural study, the ERα LBD has been observed to bind NR box3 of transcriptional intermediary factor (TIF)-2 untypically via L XX YL, whereas the ERRα LBD binds this region of TIF-2 only poorly. Here we present a new crystal structure of the ERRα LBD in complex with a PGC-1α box3 peptide. In this structure, residues N-terminal of the PGC-1α L XX YL motif formed contacts with helix 4, the loop connecting helices 8 and 9, and with the C terminus of the ERRα LBD. Interaction studies using wild-type and mutant PGC-1α and ERRα showed that these contacts are functionally relevant and are required for efficient ERRα/PGC-1α interaction. Furthermore, a structure comparison between ERRα and ERα and mutation analyses provided evidence that the helix 8–9 loop, which differs significantly in both nuclear receptors, is a major determinant of coactivator binding specificity. Finally, our results revealed that in ERRα the helix 8–9 loop allosterically links the LBD homodimer interface with the coactivator cleft, thus providing a plausible explanation for distinct PGC-1α binding to ERRα monomers and homodimers.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0021925820596774; http://dx.doi.org/10.1074/jbc.m801920200; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=50649109865&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/18441008; https://linkinghub.elsevier.com/retrieve/pii/S0021925820596774; http://www.jbc.org/lookup/doi/10.1074/jbc.M801920200; https://syndication.highwire.org/content/doi/10.1074/jbc.M801920200; https://dx.doi.org/10.1074/jbc.m801920200
Elsevier BV
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