Structural and functional analysis of the N-terminal region of death receptor 5.
- Author:
Zhang FENG
1
;
Chen CAI-FENG
;
Liu SHI-LIAN
;
Zheng DE-XIAN
;
Liu YAN-XIN
Author Information
- Publication Type:Journal Article
- MeSH: Animals; Antibodies, Monoclonal; chemistry; Binding Sites; Gene Deletion; Genetic Engineering; Genetic Vectors; Humans; Mice; Protein Binding; Receptors, TNF-Related Apoptosis-Inducing Ligand; chemistry; genetics; metabolism
- From: Acta Academiae Medicinae Sinicae 2011;33(1):33-38
- CountryChina
- Language:English
-
Abstract:
OBJECTIVETo investigate the structure and function of the N-terminal region (NTR) of death receptor 5 (DR5).
METHODSA series of deletions of the DR5 extracellular domain (DR5-ECD) proteins were expressed in E.coli. and purified by affinity chromatography. The binding ability of these deletant proteins to AD5-10, a mouse anti-human DR5 monoclonal antibody, was evaluated by immunoblotting and ELISA.
RESULTSRecombinant DR5-ECD proteins containing the NTR were recognized and bound by AD5-10, while the other deletant proteins without the NTR failed to interact with AD5-10.
CONCLUSIONThere is an AD5-10 targeting site in the NTR of DR5, which may play a role in developing novel immunotherapies for cancers.
