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
en 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.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Serpinas
/
Ixodes
/
Inhibidores Enzimáticos
/
Antiinflamatorios
Límite:
Animals
Idioma:
En
Revista:
Acta Crystallogr D Struct Biol
Año:
2021
Tipo del documento:
Article
País de afiliación:
República Checa