1gqv
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. 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 Page seeded by OCA on Fri May 2 17:54:33 2008