Helmholtz Zentrum Munchen receives funds from The Michael J. Fox Foundation

This press release is available in German.

Starting in August 2010, an innovative project will be funded at Helmholtz Zentrum München which could pave the way for an effective therapy for PD. The aim of the project is to obtain a crystal structure of the kinase domain of the LRRK2 protein and describe its biochemical and enzymatic functions.

Professor Michael Sattler, director of the Institute of Structural Biology, Professor Marius Ueffing, head of the Department of Protein Science and Dr. Johannes Gloeckner led by Dr. Alex Burgin at Emerald Biostructures want to develop new methods in order to be able to purify and biochemically characterize larger quantities of the protein or its relevant domains. Biochemical methods shall be combined with NMR spectroscopy, small-angle X-ray scattering experiments, and ultimately X-ray crystal structure analysis in order to decode the spatial structure of the protein. "Solving the structure of the enzyme believed to be a key molecular mechanism behind Parkinson's disease could revolutionize the field," said Dr. Burgin, Emerald BioStructures.

LRRK2 (leucine-rich repeat kinase 2) is considered to be the central factor in the development of a genetic form of PD. The hyperactivity of the enzyme could lead to increased loss of neurons in the midbrain, which is characteristic of this common neurodegenerative disease.

"When the structure of LRRK2 is known, we will have legitimate hope for developing new therapeutic approaches, at least for LRRK2-associated PD," said Professor Sattler. Knowledge of the protein structure is a prerequisite for rationally developing and optimizing active substances against Parkinson's. "At the same time," he added, "we will gain new insights into how Parkinson's develops, enabling an intervention at earlier stages in the future."

Provided by Helmholtz Zentrum München - German Research Center for Environmental Health