Structural and functional analysis of the N-terminal region of death receptor 5 / 中国医学科学院学报
Acta Academiae Medicinae Sinicae
;
(6): 33-38, 2011.
Article
in English
| WPRIM
| ID: wpr-341463
ABSTRACT
<p><b>OBJECTIVE</b>To investigate the structure and function of the N-terminal region (NTR) of death receptor 5 (DR5).</p><p><b>METHODS</b>A 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.</p><p><b>RESULTS</b>Recombinant 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.</p><p><b>CONCLUSION</b>There is an AD5-10 targeting site in the NTR of DR5, which may play a role in developing novel immunotherapies for cancers.</p>
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Protein Binding
/
Binding Sites
/
Genetic Engineering
/
Chemistry
/
Gene Deletion
/
Receptors, TNF-Related Apoptosis-Inducing Ligand
/
Genetic Vectors
/
Genetics
/
Metabolism
/
Antibodies, Monoclonal
Limits:
Animals
/
Humans
Language:
English
Journal:
Acta Academiae Medicinae Sinicae
Year:
2011
Type:
Article
Similar
MEDLINE
...
LILACS
LIS