 These two sites are located on the convex surface of Hop TPR2  and involved in interactions with  Hsp90 middle and C-terminal domains. Motif analysis was combined with phylogenetic trees and structural mapping to investigate the evolutionary conservation of important structural and functional sites of Hop. Statistical coupling analysis identified several sectors of coevolving residues in Hop. The convex sites of interaction between Hop TPR2 and Hsp90 middle and C-terminal domains were found to be part of separately coevolving sectors. This provides further evidence that these convex interaction sites are important to complex formation with Hsp90, and are thus potential sites for inhibitor design (in addition to the concave sites which have been the focus of previous efforts) .
<clarity>  These two sites are located on the convex surface of Hop TPR2  and involved in interactions with  Hsp90 middle and C-terminal domains. Motif analysis was combined with phylogenetic trees and structural mapping to investigate the evolutionary conservation of important structural and functional sites of Hop. Statistical coupling analysis identified several sectors of coevolving residues in Hop. The convex sites of interaction between Hop TPR2 and Hsp90 middle and C-terminal domains were found to be part of separately coevolving sectors. This provides further evidence that these convex interaction sites are important to complex formation with Hsp90, and are thus potential sites for inhibitor design (in addition to the concave sites which have been the focus of previous efforts) .
 These two sites are located on the convex surface of Hop TPR2 and involved in interactions with Hsp90 middle domain. Since the convex sites are less conserved than the concave sites, it makes their potential for malarial inhibitor design extremely attractive (as opposed to the concave sites which have been the focus of previous efforts) .