title: Engineering aspartic proteases to probe structure and function relationships.
abstract: Recently, protein engineering has been used to interconvert homodimeric and homologous single-chain aspartic proteases, with some success. The independent folding of the domains of these proteases has also permitted the engineering of domain-rearranged protease zymogens and the use of individual domains as probes for structural denaturation. In addition, site-directed mutagenesis has provided insights into the catalytic mechanism and specificity of this family of proteases.
authors.affiliation: Oklahoma Medical Research Foundation, Oklahoma City.
authors.forename: J
authors.initials: J
authors.lastname: Tang
authors.forename: X
authors.initials: X
authors.lastname: Lin
mesh_terms: D016282:Aspartic Acid Endopeptidases / Q000235:genetics* / Q000378:metabolism*; D005075:Biological Evolution; D008958:Models, Molecular; D015202:Protein Engineering; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
chemical_list: D016282:Aspartic Acid Endopeptidases