Artículos de revistas
Structure of human uropepsin at 2.45 angstrom resolution
Fecha
2001-11-01Registro en:
Acta Crystallographica Section D-biological Crystallography. Copenhagen: Munksgaard Int Publ Ltd, v. 57, p. 1560-1570, 2001.
0907-4449
10.1107/S0907444901013865
WOS:000171778400010
WOS000171778400010.pdf
2835029061696580
Autor
Universidade Estadual Paulista (Unesp)
FMTM
Instituto Butantan
Institución
Resumen
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.