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Article

Unique functional and structural properties of the LRRK2 protein ATP-binding pocket.

The Journal of biological chemistry - 21 Nov 2014

Liu Zhiyong, Galemmo Robert A, Fraser Kyle B, Moehle Mark S, Sen Saurabh, Volpicelli-Daley Laura A, DeLucas Lawrence J, Ross Larry J, Valiyaveettil Jacob, Moukha-Chafiq Omar, Pathak Ashish K, Ananthan Subramaniam, Kezar Hollis, White E Lucile, Gupta Vandana, Maddry Joseph A, Suto Mark J, West Andrew B

Abstract excerpt

Pathogenic mutations in the LRRK2 gene can cause late-onset Parkinson disease. The most common mutation, G2019S, resides in the kinase domain and enhances activity. LRRK2 possesses the unique property of cis-autophosphorylation of its own GTPase domain. Because high-resolution structures of the human LRRK2 kinase domain are not available, we used novel high-throughput assays that measured both...

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PMID: 25228699
DOI: 10.1074/jbc.M114.602318
PMCID: PMC4239640

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

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