Prof. Dr. Matthias Preller and Dr. Elmar Behrmann / Institute of Biophysical Chemistry / MHH and Max Planck Institute of Molecular Physiology

Research report 2012

The cover image of the 2012 research report shows a computer-chemically generated structural model of the actomyosin-tropomyosin complex (ATM complex) of human non-muscular myosin-2B (blue), g-actin (gray) and tropomyosin (green). The model is based on the recently experimentally solved structure of an ATM complex consisting of myosin-1, tropomyosin and α-actin(Behrmann et al., Cell, 150, 327-338, 2012).

The models provide new insights into the regulation of actomyosin motor function by tropomyosin, the mechanism of chemomechanical coupling in the myosin motor domain and form the basis for the development of therapeutic approaches for the treatment of diseases caused by mutations of the contractile proteins.

In the accompanying animation, the reactive thiol region (SH1/SH2) in the myosin motor domain, which is a focal point of allosteric Communications, is also highlighted. Through the combined use of structural, computational chemistry and biophysical methods, the mechanism leading to the disruption of force development and ATP hydrolysis by the point mutations G680V and G680A could be elucidated, whereby an uncoupling of crucial structural elements in this region takes place(Preller et al., J. Biol. Chem., 286, 35051-35060, 2011).