1wlj

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spinqualitylabelsall models 1wlj, resolution 1.9Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

human ISG20

Overview

ISG20 is an interferon-induced antiviral exoribonuclease that acts on, single-stranded RNA and also has minor activity towards single-stranded, DNA. It belongs to the DEDDh group of RNases of the DEDD exonuclease, superfamily. We have solved the crystal structure of human ISG20 complexed, with two Mn2+ ions and uridine 5'-monophosphate (UMP) at 1.9 A resolution., Its structure, including that of the active site, is very similar to those, of the corresponding domains of two DEDDh-group DNases, the epsilon, subunit of Escherichia coli DNA polymerase III and E. coli exonuclease I, strongly suggesting that its catalytic mechanism is identical to that of, the two DNases. However, ISG20 also has distinctive residues, Met14 and, Arg53, to accommodate hydrogen bonds with the 2'-OH group of the UMP, ribose, and these residues may be responsible for the preference of ISG20, for RNA substrates.

About this Structure

1WLJ is a Single protein structure of sequence from Homo sapiens with MN, ACT and U5P as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of human ISG20, an interferon-induced antiviral ribonuclease., Horio T, Murai M, Inoue T, Hamasaki T, Tanaka T, Ohgi T, FEBS Lett. 2004 Nov 5;577(1-2):111-6. PMID:15527770

Page seeded by OCA on Mon Nov 12 19:52:12 2007