Crystal structure of <i>Trichinella spiralis</i> calreticulin and the structural basis of its complement evasion mechanism involving C1q.

The deuterium exchange value of the five peptides derived from C1q, including P1 (Residues 152 A –176 A : SIVSSSRGQVRRSLGFCDTTNKGLF), P2 (Residues 116 B –142 B : DHVITNMNNYEPRSGKFTCKVPGLYY), P3 (Residues 197 B –217 B : LQATDKNSLLGMEGANSIFSG), P4(residues 165 C –180 C : CGHTSKTNQVNSGGVL), and P5 (Residues 191 C –196 C : LAVNDY) demonstrated a decreasing trend when incubated with TsCRT △ .

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