Structural model of the dimeric Parkinson's protein LRRK2 reveals a compact architecture involving distant interdomain contacts.

doi:10.1073/pnas.1523708113

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Article

Structural model of the dimeric Parkinson's protein LRRK2 reveals a compact architecture involving distant interdomain contacts.

Proceedings of the National Academy of Sciences of the United States of America - 26 Jul 2016

Guaitoli Giambattista, Raimondi Francesco, Gilsbach Bernd K, Gómez-Llorente Yacob, Deyaert Egon, Renzi Fabiana, Li Xianting, Schaffner Adam, Jagtap Pravin Kumar Ankush, Boldt Karsten, von Zweydorf Felix, Gotthardt Katja, Lorimer Donald D, Yue Zhenyu, Burgin Alex, Janjic Nebojsa, Sattler Michael, Versées Wim, Ueffing Marius, Ubarretxena-Belandia Iban, Kortholt Arjan, Gloeckner Christian Johannes

Abstract excerpt

Leucine-rich repeat kinase 2 (LRRK2) is a large, multidomain protein containing two catalytic domains: a Ras of complex proteins (Roc) G-domain and a kinase domain. Mutations associated with familial and sporadic Parkinson's disease (PD) have been identified in both catalytic domains, as well as in several of its multiple putative regulatory domains. Several of these mutations have been linked to increased kinase...

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PMID: 27357661
DOI: 10.1073/pnas.1523708113
PMCID: PMC4968714

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