7tbc | pdb_00007tbc

Crystal structure of Plasmepsin X from Plasmodium falciparum in complex with WM382

spinqualitylabelsall models 7tbc, resolution 2.76Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.76Å Ligands: EDO, I0L, NAG, PG4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Plasmepsins IX (PMIX) and X (PMX) are essential aspartyl proteases for Plasmodium spp. egress, invasion, and development. WM4 and WM382 inhibit PMIX and PMX in Plasmodium falciparum and P. vivax. WM4 inhibits PMX, while WM382 is a dual inhibitor of PMIX and PMX. To understand their function, we identified protein substrates. Enzyme kinetic and structural analyses identified interactions responsible for drug specificity. PMIX and PMX have similar substrate specificity; however, there are distinct differences for peptide and protein substrates. Differences in WM4 and WM382 binding for PMIX and PMX map to variations in the S' region and engagement of the active site S3 pocket. Structures of PMX reveal interactions and mechanistic detail of drug binding important for development of clinical candidates against these targets. Basis for drug selectivity of plasmepsin IX and X inhibition in Plasmodium falciparum and vivax.,Hodder AN, Christensen J, Scally S, Triglia T, Ngo A, Birkinshaw RW, Bailey B, Favuzza P, Dietrich MH, Tham WH, Czabotar PE, Lowes K, Guo Z, Murgolo N, Lera Ruiz M, McCauley JA, Sleebs BE, Olsen D, Cowman AF Structure. 2022 Apr 11. pii: S0969-2126(22)00099-5. doi:, 10.1016/j.str.2022.03.018. PMID:35460613 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Plasmepsin

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