Literature summary for 3.4.23.39 extracted from

Friedman, R.; Caflisch, A.
Pepsinogen-like activation intermediate of plasmepsin II revealed by molecular dynamics analysis (2008), Proteins, 73, 814-827.

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Organism

Organism	UniProt	Comment	Textmining
Plasmodium falciparum	-	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
proteolytic modification	the large N-terminal displacement and the interdomain shift from the proenzyme structure to active plasmepsin are promoted by essential dynamics sampling. An intermediate, stabilized by electrostatic interactions between the catalytic dyad and the N-terminus of mature plasmepsin, is observed along all activation trajectories. The stabilizing interactions in the activation intermediate of plasmepsin are similar to those in the X-ray structure of pepsinogen. The catalytic aspartates act as hydrogen bond acceptors for the N-terminal amino group and the Ser2 hydroxyl in plasmepsin, and the side chains of Lys36pro and Tyr9 in pepsinogen	Plasmodium falciparum

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Release 2023.1 (January 2023)