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The structure of the trimer of human 4-1BB ligand is unique among members of the tumor necrosis factor superfamily.
J Biol Chem. 2010 Mar 19; 285(12):9202-10.JB

Abstract

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 4-1BB-4-1BBL 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.

Authors+Show Affiliations

Department of Biology, Yonsei University, 134 Shinchon-dong, Seodaemun-gu, Seoul 120-749, Korea.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

20032458

Citation

Won, Eun-Young, et al. "The Structure of the Trimer of Human 4-1BB Ligand Is Unique Among Members of the Tumor Necrosis Factor Superfamily." The Journal of Biological Chemistry, vol. 285, no. 12, 2010, pp. 9202-10.
Won EY, Cha K, Byun JS, et al. The structure of the trimer of human 4-1BB ligand is unique among members of the tumor necrosis factor superfamily. J Biol Chem. 2010;285(12):9202-10.
Won, E. Y., Cha, K., Byun, J. S., Kim, D. U., Shin, S., Ahn, B., Kim, Y. H., Rice, A. J., Walz, T., Kwon, B. S., & Cho, H. S. (2010). The structure of the trimer of human 4-1BB ligand is unique among members of the tumor necrosis factor superfamily. The Journal of Biological Chemistry, 285(12), 9202-10. https://doi.org/10.1074/jbc.M109.084442
Won EY, et al. The Structure of the Trimer of Human 4-1BB Ligand Is Unique Among Members of the Tumor Necrosis Factor Superfamily. J Biol Chem. 2010 Mar 19;285(12):9202-10. PubMed PMID: 20032458.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - The structure of the trimer of human 4-1BB ligand is unique among members of the tumor necrosis factor superfamily. AU - Won,Eun-Young, AU - Cha,Kiweon, AU - Byun,Jung-Sue, AU - Kim,Dong-Uk, AU - Shin,Sumi, AU - Ahn,Byungchan, AU - Kim,Young Ho, AU - Rice,Amanda J, AU - Walz,Thomas, AU - Kwon,Byoung S, AU - Cho,Hyun-Soo, Y1 - 2009/12/23/ PY - 2009/12/25/entrez PY - 2009/12/25/pubmed PY - 2010/4/13/medline SP - 9202 EP - 10 JF - The Journal of biological chemistry JO - J Biol Chem VL - 285 IS - 12 N2 - 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 4-1BB-4-1BBL 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. SN - 1083-351X UR - https://www.unboundmedicine.com/medline/citation/20032458/The_structure_of_the_trimer_of_human_4_1BB_ligand_is_unique_among_members_of_the_tumor_necrosis_factor_superfamily_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0021-9258(20)87315-3 DB - PRIME DP - Unbound Medicine ER -