Engineering aspartic proteases to probe structure and function relationships.
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.
Tang
J
J
Oklahoma Medical Research Foundation, Oklahoma City.
Lin
X
X
D016282:Aspartic Acid Endopeptidases / Q000235:genetics* / Q000378:metabolism*; D005075:Biological Evolution; D008958:Models, Molecular; D015202:Protein Engineering; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
D016282:Aspartic Acid Endopeptidases