Substrate Specificity of Cysteine Proteases Beyond the S₂ Pocket: Mutagenesis and Molecular Dynamics Investigation of Fasciola hepatica Cathepsins L.

ABSTRACT: Cysteine proteases are widespread in all life kingdoms, being central to diverse physiological processes based on a broad range of substrate specificity. Paralogous Fasciola hepatica cathepsin L proteases are essential to parasite invasion, tissue migration and reproduction. In spite of similarities in their overall sequence and structure, these enzymes often exhibit different substrate specificity. These preferences are principally determined by the amino acid composition of the active site's S₂ subsite (pocket) of the enzyme that interacts with the substrate P₂ residue (Schetcher and Berger nomenclature). Although secreted FhCL1 accommodates aliphatic residues in the S₂ pocket, FhCL2 is also efficient in cleaving proline in that posit

SUBMITTER: Corvo I 

PROVIDER: S-EPMC5917446 | biostudies-literature | 2018

REPOSITORIES: biostudies-literature