1GQV

Atomic Resolution (0.98A) Structure of Eosinophil-Derived Neurotoxin

Summary for 1GQV

• Entry DOI: 10.2210/pdb1gqv/pdb
• Related: 1HI2 1HI3 1HI4 1HI5
• Descriptor: EOSINOPHIL-DERIVED NEUROTOXIN, ACETATE ION (3 entities in total)
• Functional Keywords: rnase-2, rnase us, ribonuclease
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 1
• Total formula weight: 15670.79

Authors

Swaminathan, G.J.,Holloway, D.E.,Veluraja, K.,Acharya, K.R. (deposition date: 2001-12-05, release date: 2002-03-08, Last modification date: 2024-10-23)

Primary citation

Swaminathan, G.J.,Holloway, D.E.,Veluraja, K.,Acharya, K.R.
Atomic Resolution (0.98 A) Structure of Eosinophil-Derived Neurotoxin
Biochemistry, 41:3341-, 2002

PubMed Abstract: 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.

PubMed: 11876642
DOI: 10.1021/BI015911F

Experimental method

X-RAY DIFFRACTION (0.98 Å)