dc.contributorUniversidade Estadual Paulista (UNESP)
dc.creatorCanduri, F.
dc.creatorTeodoro, LGVL
dc.creatorFadel, V
dc.creatorLorenzi, CCB
dc.creatorHial, V
dc.creatorGomes, RAS
dc.creatorNeto, JR
dc.creatorde Azevedo, W. F.
dc.date2014-05-20T15:22:19Z
dc.date2016-10-25T17:55:58Z
dc.date2014-05-20T15:22:19Z
dc.date2016-10-25T17:55:58Z
dc.date2001-11-01
dc.date.accessioned2017-04-05T23:35:59Z
dc.date.available2017-04-05T23:35:59Z
dc.identifierActa Crystallographica Section D-biological Crystallography. Copenhagen: Munksgaard Int Publ Ltd, v. 57, p. 1560-1570, 2001.
dc.identifier0907-4449
dc.identifierhttp://hdl.handle.net/11449/33317
dc.identifierhttp://acervodigital.unesp.br/handle/11449/33317
dc.identifier10.1107/S0907444901013865
dc.identifierWOS:000171778400010
dc.identifierWOS000171778400010.pdf
dc.identifierhttp://dx.doi.org/10.1107/S0907444901013865
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/877453
dc.descriptionThe molecular structure of human uropepsin, an aspartic proteinase from the urine produced in the form of pepsinogen A in the gastric mucosa, has been determined by molecular replacement using human pepsin as the search model. Crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 50.99, b = 75.56, c = 89.90 Angstrom. Crystallographic refinement led to an R factor of 0.161 at 2.45 Angstrom resolution. The positions of 2437 non-H protein atoms in 326 residues have been determined and the model contains 143 water molecules. 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 model of the uropepsin-pepstatin complex has been constructed based on the high-resolution crystal structure of pepsin complexed with pepstatin.
dc.languageeng
dc.publisherMunksgaard Int Publ Ltd
dc.relationActa Crystallographica Section D: Biological Crystallography
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.titleStructure of human uropepsin at 2.45 angstrom resolution
dc.typeOtro


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