Structural and functional analysis of the N-terminal region of death receptor 5

Zhongguo Yi Xue Ke Xue Yuan Xue Bao. 2011 Feb;33(1):33-8. doi: 10.3881/j.issn.1000-503X.2011.01.008.

Abstract

Objective: To investigate the structure and function of the N-terminal region (NTR) of death receptor 5 (DR5).

Methods: 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.

Results: 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.

Conclusion: There is an AD5-10 targeting site in the NTR of DR5, which may play a role in developing novel immunotherapies for cancers.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antibodies, Monoclonal / chemistry
  • Binding Sites
  • Gene Deletion
  • Genetic Engineering
  • Genetic Vectors
  • Humans
  • Mice
  • Protein Binding
  • Receptors, TNF-Related Apoptosis-Inducing Ligand / chemistry*
  • Receptors, TNF-Related Apoptosis-Inducing Ligand / genetics
  • Receptors, TNF-Related Apoptosis-Inducing Ligand / metabolism

Substances

  • Antibodies, Monoclonal
  • Receptors, TNF-Related Apoptosis-Inducing Ligand
  • Tnfrsf10b protein, mouse