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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>
Subject(s)
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

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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