Below are links to the coordinates of recent depositions, pending curation by the PDB:
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4-hydroxyphenylpyruvate dioxygenase (HPPD) catalyzes the second step of tyrosine catabolism. Higher organisms utilize this pathway primarily to remove the relatively insoluble tyrosine from blood. Several diseases are associated with human HPPD including type III tyrosinemia, an autosomal recessive disorder that results in mental retardation and corneal opacities, and hawkinsinuria, an autosomal dominant disorder characterized by metabolic acidosis and failure to thrive. To provide insights into disease pathology and development of species-specific inhibitors, we have determined the crystal structure of human HPPD.
Here we report the structure of Human HPPD at 1.8 Å resolution.
The SGC has a visiting scientist program in which external scientists, graduate students and postdoctoral fellows who have a position at another institution are invited to work within the SGC on proteins of mutual interest.
Synthesis, Kinase Inhibitory Potencies, and in Vitro Antiproliferative Evaluation of New Pim Kinase Inhibitors. Akué-Gédu R, Rossignol E, Azzaro S, Knapp S, Filippakopoulos P, Bullock AN, Bain J, Cohen P, Prudhomme M, Anizon F, Moreau P. Journal of Medicinal Chemistry. (2009) 52(20):6369-6381.
