Molecular mechanics of the alpha-actinin rod domain: bending, torsional, and extensional behavior.

ABSTRACT: alpha-Actinin is an actin crosslinking molecule that can serve as a scaffold and maintain dynamic actin filament networks. As a crosslinker in the stressed cytoskeleton, alpha-actinin can retain conformation, function, and strength. alpha-Actinin has an actin binding domain and a calmodulin homology domain separated by a long rod domain. Using molecular dynamics and normal mode analysis, we suggest that the alpha-actinin rod domain has flexible terminal regions which can twist and extend under mechanical stress, yet has a highly rigid interior region stabilized by aromatic packing within each spectrin repeat, by electrostatic interactions between the spectrin repeats, and by strong salt bridges between its two anti-parallel monomers. By exploring the natural vibrations of the alpha-actinin

SUBMITTER: Golji J 

PROVIDER: S-EPMC2676514 | biostudies-literature | 2009 May

REPOSITORIES: biostudies-literature