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NTIS 바로가기Proceedings of the National Academy of Sciences of the United States of America, v.116 no.23, 2019년, pp.11229 - 11234
Flydal, Marte Innselset (Department of Biomedicine, University of Bergen, 5009 Bergen, Norway) , Alcorlo-Pagés, Martín , Johannessen, Fredrik Gullaksen (Department of Crystallography and Structural Biology, Instituto de Quí) , Martínez-Caballero, Siseth (mica-Fí) , Skjærven, Lars (sica “Rocasolano,” Consejo Superior de Investigaciones Cientí) , Fernandez-Leiro, Rafael (ficas (CSIC), 28006 Madrid, Spain) , Martinez, Aurora , Hermoso, Juan A. (Department of Biomedicine, University of Bergen, 5009 Bergen, Norway)
SignificanceThe present crystal structure of phenylalanine hydroxylase (PAH) provides the 3D structure of the full-length human PAH, both unbound and complexed with the tetrahydrobiopterin (BH4) cofactor. The BH4-bound state is physiologically relevant, keeping PAH stable and in a precatalytic state...
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