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. 2021 May 14;296:100776. doi: 10.1016/j.jbc.2021.100776

Figure 1.

Figure 1

Structural determination of the CD97–CD55 complex.A, the CD97–CD55 binding pattern and our chimeric construct. B, SDS-PAGE of individual adhesive domains of CD97 or CD55 or the chimeric CD97–24a–CD55 complex. C, size-exclusion profiles of above three proteins as well as the chimeric protein digested by TEV. The elution volume of bovine serum albumin (66 kDa) was indicted as a control. D, SAXS analysis of above three proteins and alignments with previously determined crystal structures of EMR2 (2bo2) and CD55 (1ojv) and crystal structure determined in the present study (CD97–24a–CD55 chimeric complex). Normalized structural difference (NSD) was indicated for each sample. E, superposition of the CD97–CD55 complex with previous individual monomers. Monomers of CD97 are from PDB IDs 2bo2, 2box, and 2bou. Monomers of CD55 are from PDB IDs 1ojv, 1ojy, and 1ojw. CD97 and CD55 in the complex are colored pink and green, respectively, while other monomers are in light colors. EMR, EGF module–containing mucin-like hormone receptor; SAXS, small-angle X-ray scattering.