| Autor: |
Canduri F; Departamento de Física, IBILCE, UNESP, São José do Rio Preto, SP 15054-000, Brazil., Teodoro LG, Fadel V, Lorenzi CC, Hial V, Gomes RA, Neto JR, de Azevedo WF Jr |
| Jazyk: |
angličtina |
| Zdroj: |
Acta crystallographica. Section D, Biological crystallography [Acta Crystallogr D Biol Crystallogr] 2001 Nov; Vol. 57 (Pt 11), pp. 1560-70. Date of Electronic Publication: 2001 Oct 25. |
| DOI: |
10.1107/s0907444901013865 |
| Abstrakt: |
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 A. Crystallographic refinement led to an R factor of 0.161 at 2.45 A 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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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