The three-dimensional structure of the complex of proteinase K with its naturally occurring protein inhibitor, PKI3
| Autor: | Klaus D. Jany, Demetrius Tsernoglou, Gour P. Pal, Constantin A. Kavounis |
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| Rok vydání: | 1994 |
| Předmět: |
Models
Molecular Serine Proteinase Inhibitors Stereochemistry Proteinase inhibitor Protein Conformation Biophysics Crystal structure Crystallography X-Ray Biochemistry Serine Residue (chemistry) Structural Biology Genetics Molecule Molecular replacement Single isomorphous replacement Molecular Biology Plant Proteins chemistry.chemical_classification biology Phase combination Serine Endopeptidases Cell Biology Proteinase K Crystallography Enzyme chemistry Enzyme-inhibitor complex biology.protein X-ray structure Endopeptidase K |
| Zdroj: | FEBS letters. 341(2-3) |
| ISSN: | 0014-5793 |
| Popis: | Proteinase K forms a 1:1 stable complex with its naturally occurring protein inhibitor, PKI3. The crystal structure of this complex has been determined by a combination of molecular replacement and single isomorphous replacement methods. The model comprises all of the 459 residues: 279 for proteinase K and 180 for PKI3, and it was refined to an R-factor of 19.2% at a resolution of 2.5 Å. Association of these two molecules in the complex indicates the binding of PKI3 in the substrate recognition site of the enzyme. The active serine residue of proteinase K in this complex possesses a somewhat different configuration to that found in its native structure and hence renders the enzyme inactive. |
| Databáze: | OpenAIRE |
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