1gqv
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ATOMIC RESOLUTION (0.98A) STRUCTURE OF EOSINOPHIL-DERIVED NEUROTOXIN
OverviewOverview
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.
About this StructureAbout this Structure
1GQV is a Single protein structure of sequence from Homo sapiens with ACT as ligand. Active as Pancreatic ribonuclease, with EC number 3.1.27.5 Structure known Active Site: AC1. Full crystallographic information is available from OCA.
ReferenceReference
Atomic resolution (0.98 A) structure of eosinophil-derived neurotoxin., Swaminathan GJ, Holloway DE, Veluraja K, Acharya KR, Biochemistry. 2002 Mar 12;41(10):3341-52. PMID:11876642
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