title: Molecular model for the binary complex of uropepsin and pepstatin.
abstract: The three-dimensional structure of human uropepsin complexed with pepstatin has been modelled using human pepsin as a template. Uropepsin is an aspartic proteinase from the urine, produced in the form of pepsinogen A in the gastric mucosa. The structure is bilobal, consisting of two predominantly beta-sheet lobes which, as observed in other aspartic proteinases, are related by a pseudo twofold axis. A structural comparison between binary complexes of pepsin:pepstatin and uropepsin:pepstatin is discussed.
authors.affiliation: Departamento de Física, IBILCE, UNESP, São José do Rio Preto, SP 15054-000, Brazil.
authors.forename: W F
authors.initials: WF
authors.lastname: de Azevedo
authors.forename: F
authors.initials: F
authors.lastname: Canduri
authors.forename: V
authors.initials: V
authors.lastname: Fadel
authors.forename: L G
authors.initials: LG
authors.lastname: Teodoro
authors.forename: V
authors.initials: V
authors.lastname: Hial
authors.forename: R A
authors.initials: RA
authors.lastname: Gomes
mesh_terms: D001665:Binding Sites; D010450:Endopeptidases / Q000737:chemistry*; D006801:Humans; D006860:Hydrogen Bonding; D008958:Models, Molecular; D010436:Pepstatins / Q000737:chemistry*; D011487:Protein Conformation; D011786:Quality Control; D013379:Substrate Specificity
chemical_list: D010436:Pepstatins; C014195:Streptomyces pepsin inhibitor; D010450:Endopeptidases; C100308:uropepsin; C031375:pepstatin