Abstract
H4-1BB, the human homologue of 4-1BB, is a 256 amino acid, 27 kDa transmembrane receptor glycoprotein first identified in screens for receptors on mouse concanavalin A-activated helper and cytotoxic T-cell lines (Vinay and Kwon 2006). It was then isolated from PMA plus ionomycin-treated human peripheral T-cell cDNA libraries (Zhou et al. 1995). In humans, 4-1BB maps to chromosome 19p13.3 (Alderson et al. 1994). It is also commonly referred to as CD137, induced by lymphocyte activation (ILA), and tumor necrosis factor receptor superfamily member 9 (TNFRSF9). The receptor, 4-1BB, and its ligand, 4-1BBL, are members of the tumor necrosis factor and tumor necrosis factor receptor superfamilies, respectively (Vinay and Kwon 2012). However, unlike other members of the tumor necrosis factor superfamily, the ecto-domain of 4-1BB forms a homotrimer with an extended, three-bladed propeller structure (Won et al. 2010). 4-1BB also has a cysteine-rich extracellular domain, a transmembrane region, and a cytoplasmic domain that contains a tyrosine kinase p56lck binding site (Vinay and Kwon 2006).
Original language | English (US) |
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Title of host publication | Cancer Therapeutic Targets |
Publisher | Springer New York |
Pages | 13-20 |
Number of pages | 8 |
Volume | 1-2 |
ISBN (Electronic) | 9781441907172 |
ISBN (Print) | 9781441907165 |
DOIs | |
State | Published - Jan 1 2017 |
Externally published | Yes |
Keywords
- Anti-4-1BB monoclonal antibody (mAB)
- H4-1BB
ASJC Scopus subject areas
- General Pharmacology, Toxicology and Pharmaceutics
- General Biochemistry, Genetics and Molecular Biology
- General Medicine