The signaling phospholipid PIP 3 creates a new interaction surface on the nuclear receptor SF1

@inproceedings{Blinda2014TheSP,
  title={The signaling phospholipid PIP 3 creates a new interaction surface on the nuclear receptor SF1},
  author={Raymond D. Blinda and Elena P. Sablinb and Kristopher M. Kuchenbeckerb and Hsiu-Ju Chiuc and Ashley M. Deaconc and Debanu Dasc and Robert J. Fletterickb and Holly A. Ingrahama},
  year={2014}
}
  • Raymond D. Blinda, Elena P. Sablinb, +5 authors Holly A. Ingrahama
  • Published 2014
The signaling phosphatidylinositol lipids PI(4,5)P2 (PIP2) and PI (3,4,5)P3 (PIP3) bind nuclear receptor 5A family (NR5As), but their regulatory mechanisms remain unknown. Here, the crystal structures of human NR5A1 (steroidogenic factor-1, SF-1) ligand binding domain (LBD) bound to PIP2 and PIP3 show the lipid hydrophobic tails sequestered in the hormone pocket, as predicted. However, unlike classic nuclear receptor hormones, the phosphoinositide head groups are fully solvent-exposed and… CONTINUE READING
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