2q8o
From Proteopedia
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crystal structure of mouse GITR ligand dimer
Overview
Glucocorticoid-induced TNF receptor ligand (GITRL) is a member of the TNF, super family (TNFSF). GITRL plays an important role in controlling, regulatory T cells. The crystal structure of the mouse GITRL (mGITRL) was, determined to 1.8-A resolution. Contrary to the current paradigm that all, ligands in the TNFSF are trimeric, mGITRL associates as dimer through a, unique C terminus tethering arm. Analytical ultracentrifuge studies, revealed that in solution, the recombinant mGITRL exists as monomers at, low concentrations and as dimers at high concentrations. Biochemical, studies confirmed that the mGITRL dimer is biologically active. Removal of, the three terminal residues in the C terminus resulted in enhanced, receptor-mediated NF-kappaB activation than by the wild-type receptor, complex. However, deletion of the tethering C-terminus arm led to reduced, activity. Our studies suggest that the mGITRL may undergo a dynamic, population shift among different oligomeric forms via C terminus-mediated, conformational changes. We hypothesize that specific oligomeric forms of, GITRL may be used as a means to differentially control GITR receptor, signaling in diverse cells.
About this Structure
2Q8O is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Structural basis for ligand-mediated mouse GITR activation., Zhou Z, Tone Y, Song X, Furuuchi K, Lear JD, Waldmann H, Tone M, Greene MI, Murali R, Proc Natl Acad Sci U S A. 2008 Jan 15;105(2):641-5. Epub 2008 Jan 4. PMID:18178614
Page seeded by OCA on Wed Feb 13 08:18:09 2008
Categories: Mus musculus | Single protein | Yukiko, T. | Zhaocai, Z. | Dimer | Gitr | Tnf | Unknown function
