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Article

How Parkinson's disease-related mutations disrupt the dimerization of WD40 domain in LRRK2: a comparative molecular dynamics simulation study.

Physical chemistry chemical physics : PCCP - 23 Sept 2020

Li Xinyi, Ye Mingyu, Wang Yue, Qiu Ming, Fu Tingting, Zhang Jian, Zhou Bin, Lu Shaoyong

Abstract excerpt

The multidomain kinase enzyme leucine-rich-repeat kinase 2 (LRRK2), activated through a homodimerization manner, has been identified as an important pathogenic factor in Parkinson's disease (PD), the second most common neurodegenerative disease wordwide. The Trp-Asp-40 (WD40) domain, located in the C-terminal LRRK2, harbours one of the most frequent PD-related variants, G2385R. However, the detailed dynamics of...

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PMID: 32914822
DOI: 10.1039/d0cp03171b

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