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Structural and mechanistic basis of the interaction between a pharmacological chaperone and human phenylalanine hydroxylase |
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| Authors: | Torreblanca Renzo Lira-Navarrete Erandi Sancho Javier Hurtado-Guerrero Ramon |
| 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. |
| 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. |
| Keywords: | folding mechanisms pharmacological chaperones phenylalanine hydroxylases phenylketonuria |
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