Utilize este identificador para citar ou criar um link para este item:
http://acervodigital.unesp.br/handle/11449/33317
- Título:
- Structure of human uropepsin at 2.45 angstrom resolution
- Universidade Estadual Paulista (UNESP)
- FMTM
- Instituto Butantan
- 0907-4449
- The 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.
- 1-Nov-2001
- Acta Crystallographica Section D-biological Crystallography. Copenhagen: Munksgaard Int Publ Ltd, v. 57, p. 1560-1570, 2001.
- 1560-1570
- Munksgaard Int Publ Ltd
- http://dx.doi.org/10.1107/S0907444901013865
- Acesso restrito
- outro
- http://repositorio.unesp.br/handle/11449/33317
Não há nenhum arquivo associado com este item.
Itens do Acervo digital da UNESP são protegidos por direitos autorais reservados a menos que seja expresso o contrário.