Insights into activity and inhibition from the crystal structure of human O-GlcNAcase.
Nat Chem Biol
; 13(6): 613-615, 2017 06.
Article
em En
| MEDLINE
| ID: mdl-28346407
ABSTRACT
O-GlcNAc hydrolase (OGA) catalyzes removal of ßα-linked N-acetyl-D-glucosamine from serine and threonine residues. We report crystal structures of Homo sapiens OGA catalytic domain in apo and inhibited states, revealing a flexible dimer that displays three unique conformations and is characterized by subdomain α-helix swapping. These results identify new structural features of the substrate-binding groove adjacent to the catalytic site and open new opportunities for structural, mechanistic and drug discovery activities.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Beta-N-Acetil-Hexosaminidases
/
Modelos Biológicos
Limite:
Humans
Idioma:
En
Revista:
Nat Chem Biol
Ano de publicação:
2017
Tipo de documento:
Article