title: Opportunities for structure-based design of protease-directed drugs.
abstract: As a result of the recent enormous technological progress, experimental structure determination has become an integral part of the development of drugs against disease-related target proteins. The post-translational modification of proteins is an important regulatory process in living organisms; one such example is lytic processing by peptidases. Many different peptidases represent disease targets and are being used in structure-based drug design approaches. The development of drugs such as aliskiren and tipranavir, which inhibit renin and HIV protease, respectively, testifies to the success of this approach.
authors.affiliation: Institute for Biochemistry, University of Zürich, Winterthurer Strasse 190, 8057 Zürich, Switzerland.
authors.forename: Peer Re
authors.initials: PR
authors.lastname: Mittl
authors.forename: Markus G
authors.initials: MG
authors.lastname: Grütter
mesh_terms: D016282:Aspartic Acid Endopeptidases / Q000737:chemistry / Q000378:metabolism; D020134:Catalytic Domain; D003546:Cysteine Endopeptidases / Q000737:chemistry / Q000378:metabolism; D015195:Drug Design; D045726:Metalloproteases / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D010447:Peptide Hydrolases / Q000737:chemistry* / Q000378:metabolism*; D011487:Protein Conformation; D011499:Protein Processing, Post-Translational; D012697:Serine Endopeptidases / Q000737:chemistry / Q000378:metabolism
chemical_list: D045726:Metalloproteases; D010447:Peptide Hydrolases; D012697:Serine Endopeptidases; D003546:Cysteine Endopeptidases; D016282:Aspartic Acid Endopeptidases