Literature DB >> 7801799

Combining electron microscopy and X-ray crystallography data to study the structure of F-actin and its implications for thin-filament regulation in muscle.

R Mendelson1, E Morris.   

Abstract

The convergence of structures, all determined by independent global searches and subsequent refinement on different electron microscopy data sets, with the X-ray fiber diffraction results strongly suggests that we now have the approximately correct structure for F-actin. This consensus structure will now provide a reliable, well-defined platform upon which to study the structure and function of proteins bound to actin. Among these are capping proteins, such as severin and gelsolin, contractile proteins, such as myosin and its subfragments, and proteins involved in regulation, such as troponin and tropomyosin.

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Year:  1994        PMID: 7801799     DOI: 10.1007/978-1-4615-2578-3_2

Source DB:  PubMed          Journal:  Adv Exp Med Biol        ISSN: 0065-2598            Impact factor:   2.622


  2 in total

Review 1.  Actin and the smooth muscle regulatory proteins: a structural perspective.

Authors:  J L Hodgkinson
Journal:  J Muscle Res Cell Motil       Date:  2000-02       Impact factor: 2.698

2.  The structure of the acto-myosin subfragment 1 complex: results of searches using data from electron microscopy and x-ray crystallography.

Authors:  R Mendelson; E P Morris
Journal:  Proc Natl Acad Sci U S A       Date:  1997-08-05       Impact factor: 11.205

  2 in total

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