Structure and enzymatic functions of human CD38

Mol Med. Nov-Dec 2006;12(11-12):317-23. doi: 10.2119/2006–00086.Lee.

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.

MeSH terms

  • ADP-ribosyl Cyclase 1 / chemistry*
  • ADP-ribosyl Cyclase 1 / metabolism*
  • Animals
  • Antigens, CD / chemistry
  • Antigens, CD / metabolism
  • Aplysia / enzymology
  • Aplysia / immunology
  • Cyclic ADP-Ribose / metabolism
  • Humans
  • NADP / metabolism

Substances

  • Antigens, CD
  • Cyclic ADP-Ribose
  • NADP
  • ADP-ribosyl Cyclase 1