[HTML][HTML] Crystal structure of the HNF4α ligand binding domain in complex with endogenous fatty acid ligand
S Dhe-Paganon, K Duda, M Iwamoto, YI Chi… - Journal of Biological …, 2002 - ASBMB
HNF4α is an orphan member of the nuclear receptor family with prominent functions in liver,
gut, kidney and pancreatic β cells. We have solved the x-ray crystal structure of the HNF4α
ligand binding domain, which adopts a canonical fold. Two conformational states are
present within each homodimer: an open form with α helix 12 (α12) extended and collinear
with α10 and a closed form with α12 folded against the body of the domain. Although the
protein was crystallized without added ligands, the ligand binding pockets of both closed …
gut, kidney and pancreatic β cells. We have solved the x-ray crystal structure of the HNF4α
ligand binding domain, which adopts a canonical fold. Two conformational states are
present within each homodimer: an open form with α helix 12 (α12) extended and collinear
with α10 and a closed form with α12 folded against the body of the domain. Although the
protein was crystallized without added ligands, the ligand binding pockets of both closed …