In the older downloads, the models are only the payware, but there are some freeware files that fix some of the graphical and flight problems.Functional domains of the Toxoplasma gondii rhoptry protease ROP-2.
ROP-2, the major rhoptry protease of Toxoplasma gondii, is secreted into the parasitophorous vacuole, where it is thought to degrade host cell receptors in order to initiate host cell invasion. The zymogen form of ROP-2 (rhoptry neck protein 2) is secreted as a result of a signal peptide at the amino-terminus that directs the molecule to the host cell endoplasmic reticulum. The amino-terminal region of rhoptry neck protein 2 contains the amino-terminal intramembrane (IM) and transmembrane (TM) domains. The present study examines the function of the carboxyl-terminal region of rhoptry neck protein 2, which contains the active site, using various deletions and amino acid substitutions. The intact molecule and carboxyl-terminal peptides comprising a functional active site domain (amino acids 458-530) inhibit host cell invasion, in a dose-dependent manner, whereas a deletion of the TM region of ROP-2 (amino acids 2-367) does not inhibit invasion. Substitution of the active site residues in the active region (amino acids 458-530) of ROP-2 with their respective residues in rhoptry phospholipase A (PLA1-1) does not inhibit invasion. However, substitution with the corresponding amino acids of rhoptry acid phosphatase (RAC-1), which is known to activate ROP-1, results in a loss of invasion, indicating that the active site in ROP-2 may play a role in the activation of ROP-2./**
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