Robert borgon vinculin thesis …
α-Actinin is a rod-shaped antiparallel dimer of two 100-kDa monomers; this configuration positions its actin-binding CH motifs at either end of the rigid rod, an arrangement that allows α-actinin to efficiently cross-link actin filaments into tight bundles (, ). The central rod domain of α-actinin contains four spectrin repeats (R1 to R4), which are triple-helical coiled-coil bundles that are connected by helical linkers (, ). In α-actinin, these repeats are aligned in a symmetric fashion that allows for the formation of the rigid dimer through interactions of the R1 and R4 repeats and of the R2 and R3 repeats (, ). However, spectrin repeats can also form stable unfolded intermediates when subjected to mechanical stress (), as occurs following the formation of adhesion complexes, and the spectrin repeats of α-actinin also harbor docking sites for a number of other cytoskeletal proteins (), in particular vinculin ().
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Note: Published in Molecular and Cellular Biology ; Philippe R. J. Bois, Robert A. Borgon, Clemens Vonrhein, and Tina Izard; "Structural Dynamics of -Actinin-Vinculin Interactions"
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