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Publication : Molecular determinants of the estrogen receptor-coactivator interface.

First Author  Mak HY Year  1999
Journal  Mol Cell Biol Volume  19
Issue  5 Pages  3895-903
PubMed ID  10207113 Mgi Jnum  J:182421
Mgi Id  MGI:5315377 Doi  10.1128/mcb.19.5.3895
Citation  Mak HY, et al. (1999) Molecular determinants of the estrogen receptor-coactivator interface. Mol Cell Biol 19(5):3895-903
abstractText  Transcriptional activation by the estrogen receptor is mediated through its interaction with coactivator proteins upon ligand binding. By systematic mutagenesis, we have identified a group of conserved hydrophobic residues in the ligand binding domain that are required for binding the p160 family of coactivators. Together with helix 12 and lysine 366 at the C-terminal end of helix 3, they form a hydrophobic groove that accommodates an LXXLL motif, which is essential for mediating coactivator binding to the receptor. Furthermore, we demonstrated that the high-affinity binding of motif 2, conserved in the p160 family, is due to the presence of three basic residues N terminal to the core LXXLL motif. The recruitment of p160 coactivators to the estrogen receptor is therefore likely to depend not only on the LXXLL motif making hydrophobic interactions with the docking surface on the receptor, but also on adjacent basic residues, which may be involved in the recognition of charged residues on the receptor to allow the initial docking of the motif.
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