Structural features of heteromeric channels composed of CALHM2 and CALHM4 paralogs
Katarzyna Drożdżyk,
Martina Peter,
Raimund Dutzler
Abstract:The CALHM proteins constitute a family of large pore channels that contains six closely related paralogs in human. Two family members, CALHM1 and 3, have been associated with the release of ATP during taste sensation. Both proteins form heteromeric channels that activate at positive potential and decreased extracellular Ca
2+
concentration. Although the structures of several family members displayed large oligomeric organizations of different size, their function has in most cases remained elusive. Our previo… Show more
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