title: Structural and mechanistic basis of the interaction between a pharmacological chaperone and human phenylalanine hydroxylase.
abstract: Not without a chaperone: Pharmacological chaperones are designed to bind and ideally stabilise their target protein. Here, we elucidate the molecular mechanism of a potential pharmacological chaperone to treat phenylketonuria. The crystal structure of human phenylalanine hydroxylase with compound IV may help in the rational design of more efficient compounds to treat this disease.
authors.affiliation: Department of Biochemistry and Molecular and Cellular Biology, Institute of Biocomputation and Physics of Complex Systems (BIFI), University of Zaragoza, BIFI-IQFR (CSIC) Joint Unit, Pedro Cerbuna 12, Mariano Esquillor s/n, Campus Rio Ebro, Edificio I+D, Spain.
authors.forename: Renzo
authors.initials: R
authors.lastname: Torreblanca
authors.forename: Erandi
authors.initials: E
authors.lastname: Lira-Navarrete
authors.forename: Javier
authors.initials: J
authors.lastname: Sancho
authors.forename: Ramon
authors.initials: R
authors.lastname: Hurtado-Guerrero
mesh_terms: D006801:Humans; D007700:Kinetics; D008958:Models, Molecular; D010651:Phenylalanine Hydroxylase / Q000737:chemistry* / Q000378:metabolism*; D011485:Protein Binding; D055503:Protein Multimerization / Q000187:drug effects; D058849:Protein Refolding / Q000187:drug effects; D017433:Protein Structure, Secondary; D054852:Small Molecule Libraries / Q000378:metabolism* / Q000494:pharmacology*
chemical_list: D054852:Small Molecule Libraries; D010651:Phenylalanine Hydroxylase