Mapping selectivity and specificity of active site of plasmepsins from Plasmodium falciparum using molecular interaction field approach.
In the search for selectivity, the aspartic proteases are known to be a very difficult case because the enzymes of this family are not only sequentially but structurally also very similar. To gain insight into the selectivity and specificity of the aspartic proteases family we characterized the binding sites of four malarial aspartic protease (plasmepsin I, plasmepsin II, plasmepsin IV, P. vivax plasmepsin) and two human aspartic proteases (cathepsin D and pepsin) with the intention of identifying the regions that could be potential sites for obtaining selectivity using molecular interaction field approach.
Kumar
Amit
A
Bioinformatics Centre, IBB, University of Pune, Pune-411007, India.
Ghosh
Indira
I
D000818:Animals; D016282:Aspartic Acid Endopeptidases / Q000737:chemistry* / Q000378:metabolism*; D001665:Binding Sites; D002402:Cathepsin D / Q000737:chemistry / Q000378:metabolism*; D019295:Computational Biology / Q000379:methods; D006801:Humans; D010434:Pepsin A / Q000737:chemistry / Q000378:metabolism; D010963:Plasmodium falciparum / Q000201:enzymology*; D025941:Protein Interaction Mapping / Q000379:methods; D015800:Protozoan Proteins / Q000737:chemistry / Q000378:metabolism*; D013329:Structure-Activity Relationship
D015800:Protozoan Proteins; D016282:Aspartic Acid Endopeptidases; D010434:Pepsin A; C089643:plasmepsin; D002402:Cathepsin D