High-Resolution Cryo-EM Structure of the Cardiac Actomyosin Complex.

Autor:	Risi C; Department of Physiological Sciences, Eastern Virginia Medical School, Norfolk, VA 23507, USA., Schäfer LU; Institute of Biological Information Processing (IBI-7), Forschungszentrum Jülich, 52425 Jülich, Germany., Belknap B; Department of Physiological Sciences, Eastern Virginia Medical School, Norfolk, VA 23507, USA., Pepper I; Department of Physiological Sciences, Eastern Virginia Medical School, Norfolk, VA 23507, USA., White HD; Department of Physiological Sciences, Eastern Virginia Medical School, Norfolk, VA 23507, USA., Schröder GF; Institute of Biological Information Processing (IBI-7), Forschungszentrum Jülich, 52425 Jülich, Germany; Physics Department, Heinrich-Heine Universität Düsseldorf, 40225 Düsseldorf, Germany., Galkin VE; Department of Physiological Sciences, Eastern Virginia Medical School, Norfolk, VA 23507, USA. Electronic address: galkinve@evms.edu.
Jazyk:	angličtina
Zdroj:	Structure (London, England : 1993) [Structure] 2021 Jan 07; Vol. 29 (1), pp. 50-60.e4. Date of Electronic Publication: 2020 Oct 15.
DOI:	10.1016/j.str.2020.09.013
Abstrakt:	Heart contraction depends on a complicated array of interactions between sarcomeric proteins required to convert chemical energy into mechanical force. Cyclic interactions between actin and myosin molecules, controlled by troponin and tropomyosin, generate the sliding force between the actin-based thin and myosin-based thick filaments. Alterations in this sophisticated system due to missense mutations can lead to cardiovascular diseases. Numerous structural studies proposed pathological mechanisms of missense mutations at the myosin-myosin, actin-tropomyosin, and tropomyosin-troponin interfaces. However, despite the central role of actomyosin interactions a detailed structural description of the cardiac actomyosin interface remained unknown. Here, we report a cryo-EM structure of a cardiac actomyosin complex at 3.8 Å resolution. The structure reveals the molecular basis of cardiac diseases caused by missense mutations in myosin and actin proteins. Competing Interests: Declaration of Interests The authors declare no competing interests. (Copyright © 2020 Elsevier Ltd. All rights reserved.)
Databáze:	MEDLINE
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