Supplementary Figure 3: Significance of FN-glycan interaction in α_Vβ₃–wtFN10 structure and IE2/Thigh and βTD/βA contacts found in the α_Vβ₃–hFN10 structure.

(a) Adhesion (mean ± SD, n = 3 independent experiments) of HEK293T cells expressing αVβ3^N339S or αV^N266Qβ3^N339S to immobilized full-length FN in presence of Ca²⁺/Mg²⁺. A₅₄₀: absorbance at 540 nm. (b) Ribbon diagram showing the ionic and electrostatic interactions between β3's EGF-like domain 2 (IE2)(in pink) and αV's Thigh domain (in blue). σA weighted 2Fo-Fc map (gray, contoured at 1.0 σ) around the interacting residues is shown. The carboxyl oxygens of the β-genu residue Asp477 in β3-subunit IE2 H-bond to a carboxyl and carbonyl oxygens of Glu547 in the Thigh domain. OE1 and OE2 of the IE2 residue Glu500 H-bond to Glu550 OD1 and to Thr553 OG, respectively, with OE2 also forming a salt bridge with Lys503 of Thigh domain. (c) Ribbon diagram showing the intrachain H-bond between Ser674 in the CD loop of the βTD and Gln319 in the α6 helix of the βA domain. σA weighted 2Fo-Fc maps around Gln319 and the Asp672-Lys676 sequence is shown in gray contoured at 1.0 σ. α helices 1, 6 and 7 and strand F-α7 loop are labeled. The metal ions are colored as in supplementary Fig. 2.