Artigo
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
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.