Ontology highlight
ABSTRACT:
SUBMITTER: Koksal AC
PROVIDER: S-EPMC2665067 | biostudies-literature | 2009 Apr
REPOSITORIES: biostudies-literature
Koksal Adem C AC Nardozzi Jonathan D JD Cingolani Gino G
The Journal of biological chemistry 20090210 15
The Vaccinia virus H1 gene product, VH1, is a dual specificity phosphatase that down-regulates the cellular antiviral response by dephosphorylating STAT1. The crystal structure of VH1, determined at 1.32 A resolution, reveals a novel dimeric quaternary structure, which exposes two active sites spaced approximately 39 A away from each other. VH1 forms a stable dimer via an extensive domain swap of the N-terminal helix (residues 1-20). In vitro, VH1 can dephosphorylate activated STAT1, in a reacti ...[more]