title: Homology modeling of Entamoeba histolytica cysteine proteinases reveals the basis for cathepsin L-like structure with cathepsin B-like specificity.
authors.affiliation: Department of Pathology, University of California, San Francisco, CA, USA.
authors.forename: L S
authors.initials: LS
authors.lastname: Brinen
authors.forename: X
authors.initials: X
authors.lastname: Que
authors.forename: J H
authors.initials: JH
authors.lastname: McKerrow
authors.forename: S L
authors.initials: SL
authors.lastname: Reed
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002401:Cathepsin B / Q000378:metabolism*; D056668:Cathepsin L; D002403:Cathepsins / Q000737:chemistry*; D003546:Cysteine Endopeptidases / Q000737:chemistry / Q000378:metabolism*; D010450:Endopeptidases; D004748:Entamoeba histolytica / Q000201:enzymology*; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity
chemical_list: D002403:Cathepsins; D010450:Endopeptidases; D003546:Cysteine Endopeptidases; D002401:Cathepsin B; D056668:Cathepsin L