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Conserved noncanonical residue Gly-126 confers instability to the middle part of the tropomyosin molecule.

Abstract:

Tropomyosin (Tm) is a two-stranded α-helical coiled-coil protein with a well established role in regulation of actin cytoskeleton and muscle contraction. It is believed that many Tm functions are enabled by its flexibility whose nature has not been completely understood. We hypothesized that the well conserved non-canonical residue Gly-126 causes local destabilization of Tm. To test this, we substituted Gly-126 in skeletal muscle α-Tm either with an Ala residue, which should stabilize the Tm ...

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Publication status:
Published

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Publisher copy:
10.1074/jbc.m110.209353

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Institution:
University of Oxford
Division:
MSD
Department:
RDM
Sub department:
RDM Cardiovascular Medicine
Role:
Author
Journal:
Journal of biological chemistry
Volume:
286
Issue:
18
Pages:
15766-15772
Publication date:
2011-05-01
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
Source identifiers:
130848
Language:
English
Keywords:
Pubs id:
pubs:130848
UUID:
uuid:3cd35787-61ef-44f7-b1cb-e44ba28fcc8b
Local pid:
pubs:130848
Deposit date:
2012-12-19

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