Supplementary Materials

The PDF file includes:

  • Materials and Methods
  • Fig. S1. Structural characterization of ANGPT2 mutations.
  • Fig. S2. Characterization of the oligomerization and TIE2 binding of ANGPT2 mutants.
  • Fig. S3. A fibrinogen-based homology model of dimeric ANGPT1150–498.
  • Fig. S4. SAXS analysis of the N-terminally truncated ANGPT1150–498 and ANGPT2147–496.
  • Fig. S5. Dimeric ANGPTs are TIE2 antagonists.
  • Fig. S6. SAXS analysis of the dimeric CMP-ANGPT1 and its complex with TIE2-LBD.
  • Fig. S7. The T299M mutation is located in the dimerization interface of ANGPT2 fibrinogen–like domains and shows decreased integrin α5 binding.
  • Fig. S8. Paracrine ANGPT2 is a TIE2 antagonist in HUVECs but a weak agonist in LECs.
  • Fig. S9. ANGPT2 expression and ANGPT2-induced TIE2 activation in HUVECs.
  • Fig. S10. ANGPT2 expression and ANGPT2-induced TIE1 activation in LECs.
  • Table S1. Summary of the functional impact of the mutations found in patients with primary lymphedema.

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Other Supplementary Material for this manuscript includes the following: