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. 2022 Mar;47(3):187-188.
doi: 10.1016/j.tibs.2021.10.003. Epub 2021 Oct 28.

Closing the structure-to-function gap for LRRK2

Valerie Tokars  1 , Chuyu Chen  1 , Loukia Parisiadou  2
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Free article

Closing the structure-to-function gap for LRRK2

Valerie Tokars et al. Trends Biochem Sci. 2022 Mar.
Free article

Abstract

Variations in the LRRK2 gene represent one of the strongest genetic factors for Parkinson's disease (PD). It has become clear that structural knowledge of the encoded large multidomain LRRK2 protein will cast light on its biological function. The new study from Myasnikov, Zhu, et al. provides a high-resolution structure of the full-length LRRK2.

Keywords: Parkinson's disease; cryo-EM; full-length leucine-rich repeat kinase 2 (LRRK2); high-resolution structure.

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Conflict of interest statement

Declaration of interests The authors declare no conflicts of interest.

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