Closing the structure-to-function gap for LRRK2

Valerie Tokars; Chuyu Chen; Loukia Parisiadou

doi:10.1016/j.tibs.2021.10.003

Closing the structure-to-function gap for LRRK2

Valerie Tokars, Chuyu Chen, Loukia Parisiadou^*

^*Corresponding author for this work

Pharmacology

Research output: Contribution to journal › Short survey › peer-review

3 Scopus citations

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.

Original language	English (US)
Pages (from-to)	187-188
Number of pages	2
Journal	Trends in Biochemical Sciences
Volume	47
Issue number	3
DOIs	https://doi.org/10.1016/j.tibs.2021.10.003
State	Published - Mar 2022

Keywords

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

ASJC Scopus subject areas

Molecular Biology
Biochemistry

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10.1016/j.tibs.2021.10.003

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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",

author = "Valerie Tokars and Chuyu Chen and Loukia Parisiadou",

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AU - Tokars, Valerie

AU - Chen, Chuyu

AU - Parisiadou, Loukia

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N2 - 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.

AB - 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.

KW - Parkinson's disease

KW - cryo-EM

KW - full-length leucine-rich repeat kinase 2 (LRRK2)

KW - high-resolution structure

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Closing the structure-to-function gap for LRRK2

Abstract

Keywords

ASJC Scopus subject areas

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