Abstract
The leukocyte cell-surface antigen CD38 is a Type II transmembrane glycoprotein. CD38 is the major NAD+ glycohydrolase in mammals, and it also acts as a raft-dependent signaling molecule to promote cell proliferation or death. Recently, we identified the structural basis for CD38 tetramerization on the cell surface, which underlies the catalytic activity and the localization of CD38 in lipid rafts. The N-linked glycosylation sites are located in strategic positions to prevent further self-association of the tetramer. The glycosylation is likely to ensure the function of CD38, by regulating the cell-surface assembly.
