Structural and biochemical characterization of the novel serpin Iripin-5 from Ixodes ricinus.
Acta Crystallogr D Struct Biol
; 77(Pt 9): 1183-1196, 2021 Sep 01.
Article
em En
| MEDLINE
| ID: mdl-34473088
ABSTRACT
Iripin-5 is the main Ixodes ricinus salivary serpin, which acts as a modulator of host defence mechanisms by impairing neutrophil migration, suppressing nitric oxide production by macrophages and altering complement functions. Iripin-5 influences host immunity and shows high expression in the salivary glands. Here, the crystal structure of Iripin-5 in the most thermodynamically stable state of serpins is described. In the reactive-centre loop, the main substrate-recognition site of Iripin-5 is likely to be represented by Arg342, which implies the targeting of trypsin-like proteases. Furthermore, a computational structural analysis of selected Iripin-5-protease complexes together with interface analysis revealed the most probable residues of Iripin-5 involved in complex formation.
Palavras-chave
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Serpinas
/
Ixodes
/
Inibidores Enzimáticos
/
Anti-Inflamatórios
Limite:
Animals
Idioma:
En
Revista:
Acta Crystallogr D Struct Biol
Ano de publicação:
2021
Tipo de documento:
Article
País de afiliação:
República Tcheca