Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 285, Issue 12, Pages 9202-9210Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M109.084442
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Funding
- National Institutes of Health [GM62580]
- Korea Research Foundation [KRF-2006-005-J04502, KRF-2008-313-C00745, KRF-C00040, KRF-2005-201-E00008, KRF-2005-084E00001]
- Korea Science and Engineering Foundation
- Arthritis Foundation Innovative Research Award
- National Research Foundation of Korea [2008-313-C00745, 2006-005-J04502, 2005-201-E00008] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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Binding of the 4-1BB ligand (4-1BBL) to its receptor, 4-1BB, provides the T lymphocyte with co-stimulatory signals for survival, proliferation, and differentiation. Importantly, the 4-1BB4-1BBL pathway is a well known target for anti-cancer immunotherapy. Here we present the 2.3-A crystal structure of the extracellular domain of human 4-1BBL. The ectodomain forms a homotrimer with an extended, three-bladed propeller structure that differs from trimers formed by other members of the tumor necrosis factor (TNF) superfamily. Based on the 4-1BBL structure, we modeled its complex with 4-1BB, which was consistent with images obtained by electron microscopy, and verified the binding site by site-directed mutagenesis. This structural information will facilitate the development of immunotherapeutics targeting 4-1BB.
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