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1.
Fig. 1.

Fig. 1. From: Structural basis for ligand-mediated mouse GITR activation.

Overall structure of mGITRL. (a) Ribbon representation of mGITRL monomer structure. The conserved β-strands (A–H) and the extending C-terminus arm with an extra β-strand (I) on the end were labeled. Note that the β-strand F was interrupted. (b) Stereoview of the electron density for the C-terminal arm. The electron density omit map was contoured at 2σ levels.

Zhaocai Zhou, et al. Proc Natl Acad Sci U S A. 2008 January 15;105(2):641-645.
2.
Fig. 5.

Fig. 5. From: Structural basis for ligand-mediated mouse GITR activation.

NF-κB activation with wild-type mGITRL and its C-terminal deletion mutants. Cos cells were transfected with WT, mutant Del1, or mutant Del2 expression plasmids. NF-κB activity was measured by luciferase activity. Generated luciferase activity with each GITRL (WT, D1, or D2)/COS transfectants was compared with that generated by the COS cell transfectant with the empty vector.

Zhaocai Zhou, et al. Proc Natl Acad Sci U S A. 2008 January 15;105(2):641-645.
3.
Fig. 4.

Fig. 4. From: Structural basis for ligand-mediated mouse GITR activation.

Putative 2:2 ligand–receptor complex. (a) Molecular shape of canonical TNF trimer. Green arrow shows the putative receptor binding crevices. (b) mGITRL dimer and putative receptor binding position. (c) Model of the receptor–ligand complex based on the OX40L-OX40 complex. A model for 2:1 would be similar except one of the receptors was removed and hence is not shown.

Zhaocai Zhou, et al. Proc Natl Acad Sci U S A. 2008 January 15;105(2):641-645.
4.
Fig. 3.

Fig. 3. From: Structural basis for ligand-mediated mouse GITR activation.

Ultracentrifugation analysis of mGITRL. (Upper) Experimental radial concentration profiles (points) and fits (lines) to a monomer–dimer–trimer equilibrium model at three different speeds (15, 25, and 33 K RPM, respectively). (Lower) Calculated weight fractions of monomer (decreasing), dimer (increasing), and trimer (essentially zero) for concentrations covered in the experiment.

Zhaocai Zhou, et al. Proc Natl Acad Sci U S A. 2008 January 15;105(2):641-645.
5.
Fig. 2.

Fig. 2. From: Structural basis for ligand-mediated mouse GITR activation.

mGITRL associates as a dimer. (a) Stereoview of mGITRL dimer. Protomers A and B are yellow and pink, respectively. The C-terminus extra β-strand (I) from one protomer joins the β-sheet (A′-A-H-C-F) of the other to form an extended intermolecular β-sheet (I-A′-A-H-C-F). (b) GITRL dimer interface viewed down the 2-fold axis. Residues on the dimeric interface are highlighted in the stick model. Alterative conformations for residues Ile-164 and Met-53 of protomer A and Leu-90, Met-166 and leu169 of protomer B are shown.

Zhaocai Zhou, et al. Proc Natl Acad Sci U S A. 2008 January 15;105(2):641-645.
6.
Fig. 6.

Fig. 6. From: Structural basis for ligand-mediated mouse GITR activation.

Model for mGITRL oligomerization and signaling. mGITRL dimer stabilized by the C-terminus tether shows moderate activity, consistent with our earlier studies (15). Deletion of the anchor β-strand from the C-terminus tethering arm (Del1) is likely to induce conformational readjustments, so that mGITRL might form a trimer similar to OX40L. Thus, the mutant shows higher activity than that of dimer. Complete deletion of the C-terminus arm (Del2) will destabilize both dimers and trimers and therefore lead to a significant reduction in transcription activity.

Zhaocai Zhou, et al. Proc Natl Acad Sci U S A. 2008 January 15;105(2):641-645.

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