A fused alpha-beta "mini-spectrin" mimics the intact erythrocyte spectrin head-to-head tetramer.

ABSTRACT: Head-to-head assembly of two spectrin heterodimers to form an actin-cross-linking tetramer is a physiologically dynamic interaction that contributes to red cell membrane integrity. Recombinant beta-spectrin C-terminal and alpha-spectrin N-terminal peptides can form tetramer-like univalent complexes, but they cannot evaluate effects of the open-closed dimer interactions or lateral associations of the two-spectrin strands on tetramer formation. In this study we produced and characterized a fused "mini-spectrin dimer" containing the beta-spectrin C-terminal region linked to the alpha-spectrin N-terminal region. This fused mini-spectrin mimics structural and functional properties of intact, full-length dimers and tetramers, including lateral association of the alpha and beta subunits in the di

SUBMITTER: Harper SL 

PROVIDER: S-EPMC2856305 | biostudies-literature | 2010 Apr

REPOSITORIES: biostudies-literature