NMR resonance assignments of mouse lipocalin-type prostaglandin D synthase/prostaglandin J2 complex.
Biomol NMR Assign
; 16(2): 225-229, 2022 10.
Article
em En
| MEDLINE
| ID: mdl-35445291
ABSTRACT
Lipocalin-type prostaglandin (PG) D synthase (L-PGDS) catalyzes the isomerization of PGH2 to produce PGD2, an endogenous somenogen, in the brains of various mammalians. We recently reported that various other PGs also bind to L-PGDS, suggesting that it could serve as an extracellular carrier for PGs. Although the solution and crystal structure of L-PGDS has been determined, as has the structure of L-PGDS complexed PGH2 analog, a structural analysis of L-PGDS complexed with other PGs is needed in order to understand the mechanism responsible for the PG trapping. Here, we report the nearly complete 1H, 13C, and 15N backbone and side chain resonance assignments of the L-PGDS/PGJ2 complex and the binding site for PGJ2 on L-PGDS.
Palavras-chave
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Oxirredutases Intramoleculares
/
Lipocalinas
Limite:
Animals
Idioma:
En
Revista:
Biomol NMR Assign
Assunto da revista:
BIOLOGIA MOLECULAR
/
MEDICINA NUCLEAR
Ano de publicação:
2022
Tipo de documento:
Article
País de afiliação:
Japão
País de publicação:
HOLANDA
/
HOLLAND
/
NETHERLANDS
/
NL
/
PAISES BAJOS
/
THE NETHERLANDS