| Autor: |
Canduri, Fernanda, Teodoro, Lívia G. V. L., Fadel, Valmir, Lorenzi, Carla C. B., Hial, Valdemar, Gomes, Roseli A. S., Neto, João Ruggiero, de Azevedo, Jr., Walter F. |
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| Zdroj: |
Acta Crystallographica: Section D (Wiley-Blackwell); Nov2001, Vol. 57 Issue 11, p1560-1570, 11p |
| Abstrakt: |
The molecular structure of human uropepsin, an asp artic 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 P212121, with unit-cell parameters a = 50.99, b = 75.56, c = 89.90 Å. Crystallographic refinement led to an R factor of 0.161 at 2.45 Å 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 β-sheet lobes which, as observed in other aspartic protein ases, 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. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
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