title: [Various aspects of structural studies of aspartate proteinases].
abstract: The paper is a brief account of aspartic proteinases' structural studies developed in V.A. Engelhardt Institute of Molecular Biology during the last 3 years. The work on porcine pepsin has been finalized after the refinement of the monoclinic crystal form at 1.8 A resolution performed in collaboration with the group of protein structure and function studies of the University of Alberta in Canada. An important structural property of chymosin which explains the enzyme specificity has been found. Protein engineering work on chymosin is being developed. The structural template for aspartic proteinases has been elucidated and on the basis of this template the model of HIV-1 protease molecule has been built. Some approaches to the design of HIV-1 protease inhibitors were elucidated.
authors.forename: N S
authors.initials: NS
authors.lastname: Andreeva
authors.forename: A E
authors.initials: AE
authors.lastname: Gushchina
authors.forename: A S
authors.initials: AS
authors.lastname: Zhdanov
authors.forename: I V
authors.initials: IV
authors.lastname: Pechik
authors.forename: M G
authors.initials: MG
authors.lastname: Safro
authors.forename: A A
authors.initials: AA
authors.lastname: Fedorov
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D016282:Aspartic Acid Endopeptidases; D010450:Endopeptidases / Q000032:analysis* / Q000235:genetics; D015497:HIV-1 / Q000201:enzymology; D006801:Humans; D008969:Molecular Sequence Data; D011487:Protein Conformation
chemical_list: D010450:Endopeptidases; D016282:Aspartic Acid Endopeptidases
vernacular_title: Nekotorye aspekty strukturnykh issledovaniĭ aspartatnykh proteinaz.