Expression and characterization of a variant of TACI (CRD2-shortTACIFc) in Pichia pastoris.
Protein Pept Lett
; 19(3): 315-25, 2012 Mar.
Article
en En
| MEDLINE
| ID: mdl-21933134
TACI is a member of the tumor necrosis factor receptor superfamily and serves as a key regulator of B cell function. The extracellular domain of a typical TNFR contains multiple copies of CRD, which bind in the monomermonomer interfaces of a trimeric ligand. TACI binds to two ligands, APRIL and BAFF, with high affinity and contains two CRD in its extracellular regions, while BCMA and BR3, contain a single or partial CRD for binding the two ligands. However, TACI can be classified as a single CRD receptor because the amino-terminal CRD1 doesn't contribute to ligand binding. To obtain a new variant of TACI possessing higher affinities for binding, we fused a repeat sequence of CRD2 to the N-terminus of the short form of TACI. The new APRIL antagonist peptide, CRD2-shortTACI-Fc, was designed based on the modeling 3-D complex structure of TACI and APRIL. As expected, the purified recombinant CRD2-shortTACI-Fc fusion protein could bind to APRIL in vitro and demonstrated dose-dependent inhibition of APRIL-induced proliferative activity in Raji cells. We found that CRD2-shortTACI-Fc, has a higher affinity for binding to ligands than short-TACI-Fc, which contains a single CRD2.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Pichia
/
Proteínas Recombinantes de Fusión
/
Ingeniería Genética
/
Proteína Activadora Transmembrana y Interactiva del CAML
Tipo de estudio:
Prognostic_studies
Límite:
Humans
Idioma:
En
Revista:
Protein Pept Lett
Asunto de la revista:
BIOQUIMICA
Año:
2012
Tipo del documento:
Article
Pais de publicación:
Países Bajos