Myopathy-causing Q147P TPM2 mutation shifts tropomyosin strands further towards the open position and increases the proportion of strong-binding cross-bridges during the ATPase cycle

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Myopathy-causing Q147P TPM2 mutation shifts tropomyosin strands further towards the open position and increases the proportion of strong-binding cross-bridges during the ATPase cycle

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作者：Olga E. Karpicheva^a ; Armen O. Simonyan^a ; ^b ; Nadezhda V. Kuleva^b ; Charles S. Redwood^c ; Yurii S. Borovikov^a ; ^{borovikov@incras.ru" class="auth_mail" title="E-mail the corresponding author}
关键词：TM ; Tropomyosin ; WT ; Wild-type ; S1 ; Myosin subfragment-1 ; FITC-phalloidin ; Phalloidin-fluorescein isothiocyanate ; 1 ; 5-IAEDANS ; N-(iodoacetaminoethyl)-1-naphthyl-amine-5-sulfonic acid ; 5-IAF ; 5-iodoacetamidofluorescein ; SDS ; &minus ; ; PAGE ; Polyacrylamide gel electrophoresis with sodium dodecyl sulfate
刊名：Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
出版年：2016
出版时间：March 2016
年：2016
卷：1864
期：3
页码：260-267
全文大小：1117 K

文摘

•: 5">Despite low affinity in solution, Q147P tropomyosin binds with actin in muscle fiber.
•: The mutation shifts tropomyosin strands closer to the center of the actin filament.
•: 5">The mutant tropomyosin increases the proportion of the strong-binding myosin heads.
•: These structural changes underlie contractile abnormalities at the congenital myopathy.