Journal article
Analysis of LRRK2 accessory repeat domains: Prediction of repeat length, number and sites of Parkinson's disease mutations
RD Mills, TD Mulhern, HC Cheng, JG Culvenor
Biochemical Society Transactions | Published : 2012
DOI: 10.1042/BST20120088
Abstract
Various investigators have identified the major domain organization of LRRK2 (leucine-rich repeat kinase 2), which includes a GTPase ROC (Ras of complex proteins) domain followed by a COR (C-terminal of ROC) domain and a protein kinase domain. In addition, there are four domains composed of structural repeat motifs likely to be involved in regulation and localization of this complex protein. In the present paper, we report our bioinformatic analyses of the human LRRK2 amino acid sequence to predict the repeat size, number and likely boundaries for the armadillo repeat, ankyrin repeat, the leucine-rich repeat and WD40 repeat regions of LRRK2. Homology modelling using known protein structures ..
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Awarded by Australian National Health and Medical Research Council
Funding Acknowledgements
We thank the Australian National Health and Medical Research Council [project grant number 566743] and the Australian Brain Foundation for financial support. R. D. M. was supported by an Australian Postgraduate Research Award, a Dowd Neuroscience Fellowship and an Australian Institute of Nuclear Science and Engineering Award.