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Figure 4 | Malaria Journal

Figure 4

From: Artemisinin resistance in rodent malaria - mutation in the AP2 adaptor μ-chain suggests involvement of endocytosis and membrane protein trafficking

Figure 4

I568T mutation in AP2 μ-chain interacts with YXXΦ motif on cargo protein. A. Rat (P84092) V401 is homologous to P. chabaudi AP2 μ-chain I568, and contributes to the hydrophobic pocket that binds L9 residue of bound peptide (DEEYGYECL) in structure 2PR9. B. Homology model for P. chabaudi wild-type homologue shows similar structure with I568 corresponding to rat V401. C. Homology model for P. falciparum orthologue shows similar structure, with I592 corresponding to rat V401 and P. chabaudi I568. D. Homology model for P. chabaudi mutant - 568T is predicted to reduce the hydrophobic character of the binding pocket in which peptide L9 binds. Note increased polar character associated with threonine hydroxyl group in D relative to B.

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