Cryo-EM structures of cardiac thin filaments reveal the 3D architecture of troponin期刊界 All Journals 搜尽天下杂志传播学术成果专业期刊搜索期刊信息化学术搜索

按检索

Cryo-EM structures of cardiac thin filaments reveal the 3D architecture of troponin

Institution:	1. Department of Anatomy and Structural Biology, Graduate School of Medicine, University of Yamanashi, 1110 Shimokato, Chuo, Yamanashi 409-3898, Japan;2. Department of Cell Biology and Anatomy, Graduate School of Medicine, the University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan;3. The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan;1. Centro de Biología Estructural, Instituto Venezolano de Investigaciones Científicas (IVIC), Apdo. 20632, Caracas 1020A, Venezuela;2. Institute of Molecular Biophysics, Florida State University, 91 Chieftan way, Tallahassee, FL 32306-4380, USA;1. Department of Physiological Sciences, Eastern Virginia Medical School, 700 West Olney Road, Lewis Hall, Room 3126, Norfolk, VA 23507, USA;2. Department of Cellular and Molecular Medicine, University of Arizona, Tucson, AZ 85724, USA;3. Institute of Complex Systems ICS-6, Forschungszentrum Jülich, 52425 Jülich, Germany;4. Physics Department, Heinrich-Heine Universität Düsseldorf, 40225 Düsseldorf, Germany;1. Department of Physiology and Biophysics, Boston University School of Medicine, Boston, Massachusetts;1. Department of Physiological Sciences, Eastern Virginia Medical School, Norfolk, VA 23507, USA;2. Institute of Biological Information Processing (IBI-7), Forschungszentrum Jülich, 52425 Jülich, Germany;3. Physics Department, Heinrich-Heine Universität Düsseldorf, 40225 Düsseldorf, Germany;1. Department of Physiology & Biophysics, Boston University School of Medicine, Boston, Massachusetts

Abstract:	Troponin is an essential component of striated muscle and it regulates the sliding of actomyosin system in a calcium-dependent manner. Despite its importance, the structure of troponin has been elusive due to its high structural heterogeneity. In this study, we analyzed the 3D structures of murine cardiac thin filaments using a cryo-electron microscope equipped with a Volta phase plate (VPP). Contrast enhancement by a VPP enabled us to reconstruct the entire repeat of the thin filament. We determined the orientation of troponin relative to F-actin and tropomyosin, and characterized the interactions between troponin and tropomyosin. This study provides a structural basis for understanding the molecular mechanism of actomyosin system.

Keywords:	Muscle Actin Tropomyosin Single particle analysis Volta phase plate Volta phase plate"} {"#name":"keyword" "$":{"id":"k0035"} "$$":[{"#name":"text" "_":"VPP TnC"} {"#name":"keyword" "$":{"id":"k0045"} "$$":[{"#name":"text" "_":"troponin C TnT"} {"#name":"keyword" "$":{"id":"k0055"} "$$":[{"#name":"text" "_":"troponin T TnI"} {"#name":"keyword" "$":{"id":"k0065"} "$$":[{"#name":"text" "_":"troponin I IT arm"} {"#name":"keyword" "$":{"id":"k0075"} "$$":[{"#name":"text" "_":"TnI-TnT arm Fourier shell correlation"} {"#name":"keyword" "$":{"id":"k0085"} "$$":[{"#name":"text" "_":"FSC
本文献已被 ScienceDirect 等数据库收录！

设为首页 | 免责声明 | 关于勤云 | 加入收藏