Supplementary Materials

Supplementary Materials for:

Manipulation of receptor oligomerization as a strategy to inhibit signaling by TNF superfamily members

Julia T. Warren, Christopher A. Nelson, Corinne E. Decker, Wei Zou, Daved H. Fremont,* Steven L. Teitelbaum*

*Corresponding author. E-mail: fremont@pathology.wustl.edu (D.H.F.); teitelbs@wustl.edu (S.L.T.)

This PDF file includes:

  • Fig. S1. Effect of solubility mutations on RANKL function.
  • Fig. S2. Comparison of wild-type htRANKL and scRANKL.
  • Fig. S3. Design of RANKL mutants that prevent binding to RANK.
  • Fig. S4. Ability of scRANKL variants to inhibit wild-type htRANKL–induced osteoclastogenesis.
  • Fig. S5. Reversion mutagenesis of YSD htRANKL clones.
  • Fig. S6. Identification of htRANKL mutants with prolonged off-rates and decreased binding to OPG by a competitive OPG screen.
  • Fig. S7. Effect of htRANKL solubility mutations on binding to OPG.
  • Fig. S8. Van der Waals surface model of wild-type htRANKL oriented to show the binding cleft.
  • Fig. S9. Combined mutations of htRANKL that block binding to RANK and OPG.
  • Fig. S10. Effects of single-block, RANKhigh on cell number and signaling.

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Citation: J. T. Warren, C. A. Nelson, C. E. Decker, W. Zou, D. H. Fremont, S. L. Teitelbaum, Manipulation of receptor oligomerization as a strategy to inhibit signaling by TNF superfamily members. Sci. Signal. 7, ra80 (2014).

© 2014 American Association for the Advancement of Science