Crystal structure of the substrate-recognition domain of the Shigella E3 ligase IpaH9.8.
Acta Crystallogr F Struct Biol Commun
; 72(Pt 4): 269-75, 2016 Apr.
Article
en En
| MEDLINE
| ID: mdl-27050259
ABSTRACT
Infectious diseases caused by bacteria have significant impacts on global public health. During infection, pathogenic bacteria deliver a variety of virulence factors, called effectors, into host cells. The Shigella effector IpaH9.8 functions as an ubiquitin ligase, ubiquitinating the NF-κB essential modulator (NEMO)/IKK-γ to inhibit host inflammatory responses. IpaH9.8 contains leucine-rich repeats (LRRs) involved in substrate recognition and an E3 ligase domain. To elucidate the structural basis of the function of IpaH9.8, the crystal structure of the LRR domain of Shigella IpaH9.8 was determined and this structure was compared with the known structures of other IpaH family members. This model provides insights into the structural features involved in substrate specificity.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Shigella
/
Ubiquitina-Proteína Ligasas
Tipo de estudio:
Prognostic_studies
Idioma:
En
Revista:
Acta Crystallogr F Struct Biol Commun
Año:
2016
Tipo del documento:
Article
País de afiliación:
Japón