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The nemaline myopathy-causing E117K mutation in β-tropomyosin reduces thin filament activation.

Abstract:

The effect of the nemaline myopathy-causing E117K mutation in β-tropomyosin (TM) on the structure and function of this regulatory protein was studied. The E117K mutant was found to have indistinguishable actin affinity compared with wild-type (WT) and similar secondary structure as measured by circular dichroism. However the E117K mutation significantly lowered maximum activation of actomyosin ATPase. To explain the molecular mechanism of impaired ATPase activation, WT and E117K TMs were cova...

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Publication status:
Published

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Publisher copy:
10.1016/j.abb.2013.05.001

Authors


Karpicheva, OE More by this author
Robinson, P More by this author
Borovikov, YS More by this author
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, RDM, Cardiovascular Medicine, BHF Centre of Research Excellence
Journal:
Archives of biochemistry and biophysics
Volume:
536
Issue:
1
Pages:
25-30
Publication date:
2013-08-05
DOI:
EISSN:
1096-0384
ISSN:
0003-9861
URN:
uuid:b309f7f7-96a4-407c-be75-a0802a464530
Source identifiers:
401933
Local pid:
pubs:401933

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