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| {{STRUCTURE_1gqv| PDB=1gqv | SCENE= }} | | {{STRUCTURE_1gqv| PDB=1gqv | SCENE= }} |
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| '''ATOMIC RESOLUTION (0.98A) STRUCTURE OF EOSINOPHIL-DERIVED NEUROTOXIN'''
| | ===ATOMIC RESOLUTION (0.98A) STRUCTURE OF EOSINOPHIL-DERIVED NEUROTOXIN=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_11876642}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 11876642 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_11876642}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Rnase us]] | | [[Category: Rnase us]] |
| [[Category: Rnase-2]] | | [[Category: Rnase-2]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:54:33 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 05:55:34 2008'' |