title: Crystal structure of the catalytic domain of human phenylalanine hydroxylase reveals the structural basis for phenylketonuria.
abstract: The 2.0 A crystal structure of the catalytic domain of human phenylalanine hydroxylase reveals a fold similar to that of tyrosine hydroxylase. It provides the first structural view of where mutations occur and a rationale to explain molecular mechanisms of the enzymatic phenotypes in the autosomal recessive disorder phenylketoneuria.
authors.forename: H
authors.initials: H
authors.lastname: Erlandsen
authors.forename: F
authors.initials: F
authors.lastname: Fusetti
authors.forename: A
authors.initials: A
authors.lastname: Martinez
authors.forename: E
authors.initials: E
authors.lastname: Hough
authors.forename: T
authors.initials: T
authors.lastname: Flatmark
authors.forename: R C
authors.initials: RC
authors.lastname: Stevens
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites / Q000235:genetics; D003460:Crystallization; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009154:Mutation; D010651:Phenylalanine Hydroxylase / Q000737:chemistry* / Q000235:genetics; D010661:Phenylketonurias / Q000201:enzymology* / Q000235:genetics; D017510:Protein Folding; D014446:Tyrosine 3-Monooxygenase / Q000737:chemistry / Q000235:genetics
chemical_list: D010651:Phenylalanine Hydroxylase; D014446:Tyrosine 3-Monooxygenase