Article
Myopathy-causing mutation R91P in the TPM3 gene drastically impairs structural and functional properties of slow skeletal muscle tropomyosin γβ-heterodimer.
Archives of biochemistry and biophysics - 1 Feb 2024
Gonchar Anastasiia D, Koubassova Natalia A, Kopylova Galina V, Kochurova Anastasia M, Nefedova Victoria V, Yampolskaya Daria S, Shchepkin Daniil V, Bershitsky Sergey Y, Tsaturyan Andrey K, Matyushenko Alexander M, Levitsky Dmitrii I
Abstract excerpt
Tropomyosin (Tpm) is a regulatory actin-binding protein involved in Ca2+ activation of contraction of striated muscle. In human slow skeletal muscles, two distinct Tpm isoforms, γ and β, are present. They interact to form three types of dimeric Tpm molecules: γγ-homodimers, γβ-heterodimers, or ββ-homodimers, and a majority of the molecules are present as γβ-Tpm heterodimers. Point mutation R91P within the TPM3...
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