Literature DB >> 19321455

Structure and orientation of troponin in the thin filament.

Danielle M Paul1, Edward P Morris, Robert W Kensler, John M Squire.   

Abstract

The troponin complex on the thin filament plays a crucial role in the regulation of muscle contraction. However, the precise location of troponin relative to actin and tropomyosin remains uncertain. We have developed a method of reconstructing thin filaments using single particle analysis that does not impose the helical symmetry of actin and is independent of a starting model. We present a single particle three-dimensional reconstruction of the thin filament. Atomic models of the F-actin filament were fitted into the electron density maps and troponin and tropomyosin located. The structure provides evidence that the globular head region of troponin labels the two strands of actin with a 27.5-A axial stagger. The density attributed to troponin appears tapered with the widest point toward the barbed end. This leads us to interpret the polarity of the troponin complex in the thin filament as reversed with respect to the widely accepted model.

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Year:  2009        PMID: 19321455      PMCID: PMC2685683          DOI: 10.1074/jbc.M808615200

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  55 in total

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  20 in total

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Review 4.  Historical perspective on heart function: the Frank-Starling Law.

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Review 8.  New insights into the regulation of the actin cytoskeleton by tropomyosin.

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9.  Structure of the tropomyosin overlap complex from chicken smooth muscle: insight into the diversity of N-terminal recognition.

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10.  A novel approach to the structural analysis of partially decorated actin based filaments.

Authors:  Danielle M Paul; John M Squire; Edward P Morris
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