Atomic Resolution (0.98 Å) Structure of Eosinophil-Derived Neurotoxin
| Autor: | Daniel E. Holloway, K.R. Acharya, G. J. Swaminathan, K. Veluraja |
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| Rok vydání: | 2002 |
| Předmět: |
Models
Molecular Binding Sites biology Protein Conformation Structural similarity Chemistry Stereochemistry Resolution (electron density) Eosinophil-derived neurotoxin Eosinophil-Derived Neurotoxin Crystal structure Crystallography X-Ray Biochemistry Recombinant Proteins Crystallography Ribonucleases Protein structure Catalytic Domain Catalytic triad biology.protein Ribonuclease Binding site |
| Zdroj: | Biochemistry. 41:3341-3352 |
| ISSN: | 1520-4995 0006-2960 |
| DOI: | 10.1021/bi015911f |
| Popis: | Human eosinophil-derived neurotoxin (EDN) is a small, basic protein that belongs to the ribonuclease A superfamily. EDN displays antiviral activity and causes the neurotoxic Gordon phenomenon when injected into rabbits. Although EDN and ribonuclease A have appreciable structural similarity and a conserved catalytic triad, their peripheral substrate-binding sites are not conserved. The crystal structure of recombinant EDN (rEDN) has been determined at 0.98 A resolution from data collected at a low temperature (100 K). We have refined the crystallographic model of the structure using anisotropic displacement parameters to a conventional R-factor of 0.116. This represents the highest resolution structure of rEDN determined to date and is only the second ribonuclease structure to be determined at a resolution greater than 1.0 A. The structure provides a detailed picture of the conformational freedom at the various subsites of rEDN, and the water structure accounts for more than 50% of the total solvent content of the unit cell. This information will be crucial for the design of tight-binding inhibitors to restrain the ribonucleolytic activity of rEDN. |
| Databáze: | OpenAIRE |
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