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Biochem Biophys Res Commun. 2010 Feb 19;392(4):490-4. doi: 10.1016/j.bbrc.2010.01.046. Epub 2010 Jan 15.

Ankyrin recognizes both surface character and shape of the 14-15 di-repeat of beta-spectrin.

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University of Illinois at Chicago, Department of Biochemistry and Molecular Genetics, 900 S. Ashland Ave., MBRB 1170, Chicago, IL 60607, USA.


The spectrin-based cytoskeleton is critical for cell stability, membrane organization and membrane protein trafficking. At its core is the high-affinity complex between beta-spectrin and ankyrin. Defects in either of these proteins may cause hemolytic disease, developmental disorders, neurologic disease, and cancer. Crystal structures of the minimal recognition motifs of ankyrin and beta-spectrin have been determined and distinct recognition mechanisms proposed. One focused on the complementary surface charges of the minimal recognition motifs, whereas the other identified an unusual kink between beta-spectrin repeats and suggested a conformation-sensitive binding surface. Using isothermal titration calorimetry and site-directed mutagenesis, we demonstrate the primacy of the inter-repeat kink as the critical determinant underlying spectrin's ankyrin affinity. The clinical implications of this are discussed in light of recognized linker mutations and polymorphisms in the beta-spectrins.

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