Structure and enzymatic functions of human CD38.
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 Ca(2+) messengers targeting, respectively, the endoplasmic reticulum and lysosomal Ca(2+) stores. The protein has recently been crystallized and its three-dimensional structure solved to a resolution of 1.9 A. 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.
Lee
Hon Cheung
HC
Department of Pharmacology, University of Minnesota, Minneapolis, MN 55455, USA. leehc@hku.hk
D051997:ADP-ribosyl Cyclase 1 / Q000737:chemistry* / Q000378:metabolism*; D000818:Animals; D015703:Antigens, CD / Q000737:chemistry / Q000378:metabolism; D001048:Aplysia / Q000201:enzymology / Q000276:immunology; D036563:Cyclic ADP-Ribose / Q000378:metabolism; D006801:Humans; D009249:NADP / Q000378:metabolism
D015703:Antigens, CD; D036563:Cyclic ADP-Ribose; D009249:NADP; D051997:ADP-ribosyl Cyclase 1