Journal Article

FZJ-2021-05896

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png High-Resolution Cryo-EM Structure of the Cardiac Actomyosin Complex

Risi, C. ; Schäfer, L. U.FZJ* ; Belknap, B. ; Pepper, I. ; White, H. D. ; Schröder, G. F.FZJ* ; Galkin, V. E. (Corresponding author)

2021
Cell Press Cambridge, Mass.

This record in other databases:      

Please use a persistent id in citations: http://hdl.handle.net/2128/31162  doi:10.1016/j.str.2020.09.013

Abstract: 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.

---

Contributing Institute(s):

1. Strukturbiochemie (IBI-7)

Research Program(s):

1. 5244 - Information Processing in Neuronal Networks (POF4-524) (POF4-524)

Appears in the scientific report 2021

---

Database coverage:
; ; BIOSIS Previews ; Biological Abstracts ; Clarivate Analytics Master Journal List ; Current Contents - Life Sciences ; Ebsco Academic Search ; Essential Science Indicators ; Nationallizenz ; SCOPUS ; Science Citation Index Expanded ; Web of Science Core Collection

---