파킨슨병 원인 단백질인 DJ-1의 3가지 구조 상태

Abstract

DJ-1 is engaged in diverse cellular processes including cellular transformation, control of protein-RNA interaction, modulation of androgen receptor, antioxidative response, sperm fertilization, and autosomal recessive early-onset parkinsonism. Although it is not clear how DJ-1 participates in various cellular processes, structural alteration can be one of the molecular bases underlying the functional feature of DJ-1. DJ-1 forms filamentous aggregates in the presence of inorganic phosphate whereas DJ-1 normally exists as a homodimeric protein. In addition, the deletion of C-terminal fifteen residues leads to the oligomerization of DJ-1. Here, we depict the details of the three distinct structural phases of DJ-1 revealed by X-ray crystallography and electron microscopy, and investigate their functional consequences.nsonism. Although it is not clear how DJ-1 participates in various cellular processes, structural alteration can be one of the molecular bases underlying the functional feature of DJ-1. DJ-1 forms filamentous aggregates in the presence of inorganic phosphate whereas DJ-1 normally exists as a homodimeric protein. In addition, the deletion of C-terminal fifteen residues leads to the oligomerization of DJ-1. Here, we depict the details of the three distinct structural phases of DJ-1 revealed by X-ray crystallography and electron microscopy, and investigate their functional consequences.