1wlj: Difference between revisions

Line 4:

==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.

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==

Line 24:

[[Category: exoribonuclease]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri~~ Feb 15 17:07:41 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:45:40 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 4: / Line 4: @@
 ==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.
+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==
@@ Line 24: / Line 24: @@
 [[Category: exoribonuclease]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:07:41 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:45:40 2008''