1wlj | pdb_00001wlj
|
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
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