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Protein Structure and Folding
1 Results
- Protein Structure and FoldingOpen Access
Crystal structure of murine 4-1BB and its interaction with 4-1BBL support a role for galectin-9 in 4-1BB signaling
Journal of Biological ChemistryVol. 293Issue 4p1317–1329Published online: December 14, 2017- Aruna Bitra
- Tzanko Doukov
- Jing Wang
- Gaelle Picarda
- Chris A. Benedict
- Michael Croft
- and others
Cited in Scopus: 254-1BB (CD137) is a TNF receptor superfamily (TNFRSF) member that is thought to undergo receptor trimerization upon binding to its trimeric TNF superfamily ligand (4-1BBL) to stimulate immune responses. 4-1BB also can bind to the tandem repeat–type lectin galectin-9 (Gal-9), and signaling through mouse (m)4-1BB is reduced in galectin-9 (Gal-9)–deficient mice, suggesting a pivotal role of Gal-9 in m4-1BB activation. Here, using sulfur-SAD phasing, we determined the crystal structure of m4-1BB to 2.2-Å resolution.