Location of extracellular cysteine-rich domains of 4-1BB binding to murine 4-1BB ligand and analysis of its possible structure
10.3760/cma.j.issn.0254-5101.2009.04.013
- VernacularTitle:小鼠4-1 BB分子的配体识别主要区域定位及结构分析
- Author:
Ling YI
;
Yanlin ZHAO
;
Xiaojue WANG
;
Pandan WEI
;
Hongtao ZHANG
- Publication Type:Journal Article
- Keywords:
Murine 4-1 BB molecule;
Cysteine-rich domain;
Recognition region of 4-1BBL
- From:
Chinese Journal of Microbiology and Immunology
2009;29(4):340-344
- CountryChina
- Language:Chinese
-
Abstract:
ObJective To locate the cysteine-rich domains(CRD) of murine 4-1BB binding to its natural ligand. Methods A serial soluble extracellular CRDs of routine 4-1BB and 4-1BBL fusion proteins was constructed and prepared. The binding of purified 4-1BB-Igs to 4-1BBL and 4-1BB monoclonal antibody were tested using ELISA assay and Western blot analysis. Blocking experiment with 4-1BBL and 4-1BB mon-oclonal antibody was performed by ELISA assay. Results All truncated overlapped proteins containing ex-tracellular CRD Ⅱ of murine 4-1BB were able to bind to 4-1BBL by ELISA assay, excepting the CRD Ⅰ do-main alone. A 4-1BB monoclonal antibody proved to block the interaction of 4-1BB and 4-1BBI, was also able to bind to CRD Ⅱ. Conclusion Murine 4-1BBL whose specificity was mapped to CRD Ⅱ of 4-1BB ex-tracellular region with a possible conformational structure.