Assistant Professor, Indiana University School of Medicine
BIOGRAPHY
MAY 04, 2016 7:00 AM PDT
Structure and function of the Parkinson's disease-associated protein LRRK2
Presented at:
2016 Gibco ExpressionWorld
Speaker
Abstract
LRRK2 is a large (2,527 amino acids) multi-domain protein consisting of 7 putative domains, including a Ras-like GTPase domain called ‘Ras of complex proteins’ (Roc) followed by a domain called C-terminal of Roc (COR), which is then followed by a kinase domain (Kin).
It remains unclear as to how perturbations of these activities results in disease; however, the most common mutation in LRRK2-associated PD, G2019S in the kinase domain, shows higher kinase activity than wild-type; therefore, its over-activation might be associated with disease pathogenesis.
We use Expi293 expression system to produce full-length LRRK2 for biochemical characterization and structural studies.
It remains unclear as to how perturbations of these activities results in disease; however, the most common mutation in LRRK2-associated PD, G2019S in the kinase domain, shows higher kinase activity than wild-type; therefore, its over-activation might be associated with disease pathogenesis.
We use Expi293 expression system to produce full-length LRRK2 for biochemical characterization and structural studies.
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