CRYSTAL-STRUCTURE OF APLYSIA ADP RIBOSYL CYCLASE, A HOMOLOG OF THE BIFUNCTIONAL ECTOZYME CD38

Citation
Gs. Prasad et al., CRYSTAL-STRUCTURE OF APLYSIA ADP RIBOSYL CYCLASE, A HOMOLOG OF THE BIFUNCTIONAL ECTOZYME CD38, Nature structural biology, 3(11), 1996, pp. 957-964
Citations number
58
Categorie Soggetti
Biology,"Cell Biology
Journal title
ISSN journal
10728368
Volume
3
Issue
11
Year of publication
1996
Pages
957 - 964
Database
ISI
SICI code
1072-8368(1996)3:11<957:COAARC>2.0.ZU;2-6
Abstract
ADP ribosyl cyclase synthesizes the novel secondary messenger cyclic A DP ribose (cADPR) utilizing NAD as a substrate. The enzyme shares exte nsive sequence similarity with two lymphocyte antigens, CD38 and BST-l ,which hydrolyse as well as synthesize cADPR. The crystal structure pr ovides a model for these cell surface enzymes. Cyclase contains two sp atially separated pockets composed of sequence conserved residues, sug gesting that the cyclization reaction may entail use of distinct sites . The enzyme dimer encloses a cavity which may entrap the intermediate , ADP ribose.