Figure 1.
Figure 1. DBL domains from EBPs and PfEMP-1. Shown are the DBL domains including the binding domains of PvDBP and PkDBP (PvRII and PkαRII); the binding domain of EBA-175 (F2), which binds sialic acid on glycophorin A; the DBLα domain of R29var1, which binds CR1; the DBLγ domain of FCR3varCSA, which binds CSA; and the DBLβC2 domain of JDP8ICAMvar, which binds ICAM-1. The position of chymotrypsin cleavage of F2 between tyrosine 531 (531Y) and lysine 532 (532K), which results in the 24-kDa F2 fragment that retains binding activity is shown. Shaded regions show the minimal deletion construct for each DBL domain that retains binding activity. Sticks under the domains show positions of cysteines. Sticks with black dots indicate cysteines that are included in the minimal functional deletion construct for each domain. The receptors the domains bind to are shown on the right; aa indicates amino acid.

DBL domains from EBPs and PfEMP-1. Shown are the DBL domains including the binding domains of PvDBP and PkDBP (PvRII and PkαRII); the binding domain of EBA-175 (F2), which binds sialic acid on glycophorin A; the DBLα domain of R29var1, which binds CR1; the DBLγ domain of FCR3varCSA, which binds CSA; and the DBLβC2 domain of JDP8ICAMvar, which binds ICAM-1. The position of chymotrypsin cleavage of F2 between tyrosine 531 (531Y) and lysine 532 (532K), which results in the 24-kDa F2 fragment that retains binding activity is shown. Shaded regions show the minimal deletion construct for each DBL domain that retains binding activity. Sticks under the domains show positions of cysteines. Sticks with black dots indicate cysteines that are included in the minimal functional deletion construct for each domain. The receptors the domains bind to are shown on the right; aa indicates amino acid.

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