Molecular model for the binary complex of uropepsin and pepstatin

dc.contributorUniversidade Estadual Paulista (UNESP)
dc.creatorde Azevedo, W. F.
dc.creatorCanduri, F.
dc.creatorFadel, V
dc.creatorTeodoro, LGVL
dc.creatorHial, V
dc.creatorGomes, RAS
dc.date2014-05-20T15:25:28Z
dc.date2016-10-25T17:59:57Z
dc.date2014-05-20T15:25:28Z
dc.date2016-10-25T17:59:57Z
dc.date2001-09-14
dc.date.accessioned2017-04-05T23:52:30Z
dc.date.available2017-04-05T23:52:30Z
dc.identifierBiochemical and Biophysical Research Communications. San Diego: Academic Press Inc., v. 287, n. 1, p. 277-281, 2001.
dc.identifier0006-291X
dc.identifierhttp://hdl.handle.net/11449/35884
dc.identifierhttp://acervodigital.unesp.br/handle/11449/35884
dc.identifier10.1006/bbrc.2001.5555
dc.identifierWOS:000171012600044
dc.identifierhttp://dx.doi.org/10.1006/bbrc.2001.5555
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/879509
dc.descriptionThe 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. (C) 2001 Academic Press.
dc.languageeng
dc.publisherAcademic Press Inc.
dc.relationBiochemical and Biophysical Research Communications
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectaspartic proteinase
dc.subjecturopepsin
dc.subjectpepstatin
dc.subjectcomplex
dc.subjectmodel
dc.subjectStructure
dc.titleMolecular model for the binary complex of uropepsin and pepstatin
dc.typeOtro


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