Structure and enzymatic functions of human CD38

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Abstract

CD38 is a novel multifunctional protein that serves not only as an antigen but also as an enzyme. It catalyzes the metabolism of cyclic ADP-ribose and nicotinic acid adenine dinucleotide phosphate, two structurally and functionally distinct Ca2+ messengers targeting, respectively, the endoplasmic reticulum and lysosomal Ca2+ stores. The protein has recently been crystallized and its three-dimensional structure solved to a resolution of 1.9 Å. The crystal structure of a binary complex reveals critical interactions between residues at the active site and a bound substrate, providing mechanistic insights to its novel multi-functional catalysis. This article reviews the current advances in the understanding of the structural determinants that control the multiple enzymatic reactions catalyzed by CD38.

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Lee, H. C. (2006). Structure and enzymatic functions of human CD38. In Molecular Medicine (Vol. 12, pp. 317–323). https://doi.org/10.2119/2006-00086.Lee

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