Fig. 2: The native structure and associated activities of CRP are evolutionarily conserved.
From: Secretory quality control constrains functional selection-associated protein structure innovation
a The pentameric assembly of purified mouse, rat, and human CRP was examined with electron microscopy and single-particle analysis. The diameters of pentameric class averages of the mouse (181 particles), rat (209 particles), and human CRP (208 particles) are 10.98, 10.97, and 10.24 nm, respectively. b The subunit structures of mouse and rat CRP were generated with SWISS-MODEL using subunit A from the crystal structure of human CRP (PDB 1B09)56 as the template. c The binding of mouse, rat, and human CRP to immobilized PC-KLH were examined with ELISA in the presence (left; n = 3 independent experiments) or absence of calcium (right; n = 6 independent experiments for mouse CRP; n = 3 independent experiments for rat and human CRP). Neither their native structures nor calcium-dependent PC-binding activities exhibited significant difference. Data are presented as mean ± SEM.
