MAY 04, 2016 07:00 AM PDT

Structure and function of the Parkinson's disease-associated protein LRRK2

  • Assistant Professor, Indiana University School of Medicine
      Dr. Hoang is an Assistant Professor in the Department of Biochemistry and Molecular Biology at Indiana University School of Medicine. His area of study is structural biology of neurodegenerative disease and structure-based drug design. He leads a team focused on understanding the mechanism of Parkinson's disease by studying the structure and function of disease-associated proteins. Dr. Hoang received his Ph.D. and B.S. from McMaster University.

    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.

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