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Figure 6.
Figure 6. Mechanism of V[NAR] Binding
(A) V[NAR] residue
Arg92 contacts AMA1 residues Asn173, Glu174, Pro185, Thr186, and
Glu187 (<4 Å) in a series of hydrogen bond and salt bridge
interactions in the 14I-1 crystallographic structure. Residue
coloring is as for Figure 5.
(B) As for (A) except for the
V[NAR] 14I1-M15 structure.
(C) V[NAR] residues Tyr94,
Tyr96, and Leu98 in the 14I-1 structure contact hydrophobic
cleft residues Phe183 and Tyr251, and associated residue Asn371,
through a network of water-mediated hydrogen bonds and potential
aromatic interactions.
(D) V[NAR] residues Leu89 and Phe100
in the 14I-1 structure are closely associated with AMA1 residues
within the hydropobic cleft (Met190, Tyr202, Met224) and
residues polymorphic between P. falciparum strains (Met190,
Phe201).
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