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Verfasst von:Li, Xiaochuan (Edward) [VerfasserIn]   i
 Orzechowski, Marek [VerfasserIn]   i
 Lehman, William [VerfasserIn]   i
 Fischer, Stefan [VerfasserIn]   i
Titel:Structure and flexibility of the tropomyosin overlap junction
Verf.angabe:Xiaochuan Edward Li, Marek Orzechowski, William Lehman, Stefan Fischer
E-Jahr:2014
Jahr:4 March 2014
Umfang:5 S.
Fussnoten:Gesehen am 26.08.2020
Titel Quelle:Enthalten in: Biochemical and biophysical research communications
Ort Quelle:Orlando, Fla. : Academic Press, 1959
Jahr Quelle:2014
Band/Heft Quelle:446(2014), 1, Seite 304-308
ISSN Quelle:1090-2104
Abstract:To be effective as a gatekeeper regulating the access of binding proteins to the actin filament, adjacent tropomyosin molecules associate head-to-tail to form a continuous super-helical cable running along the filament surface. Chimeric head-to-tail structures have been solved by NMR and X-ray crystallography for N- and C-terminal segments of smooth and striated muscle tropomyosin spliced onto non-native coiled-coil forming peptides. The resulting 4-helix complexes have a tight coiled-coil N-terminus inserted into a separated pair of C-terminal helices, with some helical unfolding of the terminal chains in the striated muscle peptides. These overlap complexes are distinctly curved, much more so than elsewhere along the superhelical tropomyosin cable. To verify whether the non-native protein adducts (needed to stabilize the coiled-coil chimeras) perturb the overlap, we carried out Molecular Dynamics simulations of head-to-tail structures having only native tropomyosin sequences. We observe that the splayed chains all refold and become helical. Significantly, the curvature of both the smooth and the striated muscle overlap domain is reduced and becomes comparable to that of the rest of the tropomyosin cable. Moreover, the measured flexibility across the junction is small. This and the reduced curvature ensure that the super-helical cable matches the contours of F-actin without manifesting localized kinking and excessive flexibility, thus enabling the high degree of cooperativity in the regulation of myosin accessibility to actin filaments.
DOI:doi:10.1016/j.bbrc.2014.02.097
URL:Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.

Volltext ; Verlag: https://doi.org/10.1016/j.bbrc.2014.02.097
 Volltext: http://www.sciencedirect.com/science/article/pii/S0006291X14003684
 DOI: https://doi.org/10.1016/j.bbrc.2014.02.097
Datenträger:Online-Ressource
Sprache:eng
Sach-SW:Actin
 Coiled-coil
 Molecular Dynamics
 Muscle regulation
 Thin filaments
K10plus-PPN:1727783964
Verknüpfungen:→ Zeitschrift

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