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The heat shock organizing protein (Hop) is important in modulating theactivity and co-interaction of two chaperones: heat shock protein 70 and 90(Hsp70 and Hsp90). Recent research suggested that Plasmodium falciparum Hop(PfHop), PfHsp70 and PfHsp90 form a complex in the trophozoite infective stage.However, there has been little computational research on the malarial Hopprotein in complex with other malarial Hsps. Using in silico characterizationof the protein, this work showed that individual domains of Hop are evolving atdifferent rates within the protein. Differences between human Hop (HsHop) andPfHop were identified by motif analysis. Homology modeling of PfHop and HsHopin complex with their own cytosolic Hsp90 and Hsp70 C-terminal peptide partnersindicated excellent conservation of the Hop concave TPR sites bound to theC-terminal motifs of partner proteins. Further, we analyzed additional bindingsites between Hop and Hsp90, and showed, for the first time, that they aredistinctly less conserved between human and malaria parasite. These sites arelocated on the convex surface of Hop TPR2, and involved in interactions withthe Hsp90 middle domain. Since the convex sites are less conserved than theconcave sites, it makes their potential for malarial inhibitor design extremelyattractive (as opposed to the concave sites which have been the focus ofprevious efforts).

Plasmodium falciparum Hop: Detailed analysis on complex formation with Hsp70 and Hsp90