Kidney and Metabolic Bone Diseases Vol.27 No.3(3)

Theme Regulation and disorders of calcium and phosphate metabolism
Title Bizzare structure capable of binding multiple targets in αKlotho
Publish Date 2014/07
Author Akihiro Imura Foundation for Biomedical Research and Innovation
[ Summary ] αKlotho (αKl) has been established as a co-receptor for the phosophate-suppressing hormone, FGF23. Various molecules including Na, K-ATPase have been independently reported to be bound to αKl. However, common binding mechanisms remain to be understood. Since αKl protein consists of repeated β-D-glycosidase-like domains, it has been hypothesized that αKl could recognize some glycoside. Indeed αKl was found to be capable of acting like a form of glucuronidase. In addition to peptide-peptide interactions, the lectin-like ability to access a sugar motif may enable the precise complex of αKl together with targets. Analysis of crystal structures may reveal how αKl can 'recognize' multiple target molecules.
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