title: Structure and enzymatic functions of human CD38.
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 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.
authors: Department of Pharmacology, University of Minnesota, Minneapolis, MN 55455, USA. leehc@hku.hk
authors: Hon Cheung
authors: HC
authors: Lee
mesh_terms: 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
chemical_list: D015703:Antigens, CD; D036563:Cyclic ADP-Ribose; D009249:NADP; D051997:ADP-ribosyl Cyclase 1