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Structural and Mechanistic Basis of the Interaction between a Pharmacological Chaperone and Human Phenylalanine Hydroxylase
Author(s) -
Torreblanca Renzo,
LiraNavarrete Erandi,
Sancho Javier,
HurtadoGuerrero Ramon
Publication year - 2012
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201200188
Subject(s) - chaperone (clinical) , phenylalanine hydroxylase , chemistry , phenylalanine , computational biology , rational design , biochemistry , biology , medicine , genetics , amino acid , pathology
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.