Stabilization of the central part of tropomyosin molecule alters the Ca2+-sensitivity of actin-myosin interactionстатья
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Статья опубликована в журнале из перечня ВАК
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 28 мая 2015 г.
Местоположение издательства:Moscow, Russia (Federation)
Первая страница:126
Последняя страница:129
Аннотация:We show that the mutations D137L and G126R, which stabilize the central part of the tropomyosin
(Tm) molecule, increase both the maximal sliding velocity of the regulated actin filaments in the in vitro motility
assay at high Са2+ concentrations and the Са2+-sensitivity of the actin-myosin interaction underlying this sliding.
Based on an analysis of the recently published data on the structure of the actin–Tm–myosin complex, we
suppose that the physiological effects of these mutations in Tm can be accounted for by their influence on the
interactions between the central part of Tm and certain sites of the myosin head