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Animal: DNA Viruses |
receptor is a homodimer
Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK1
Author for correspondence: Geoffrey L. Smith. Present address: The WrightFleming Institute, Imperial College School of Medicine, St Marys Campus, Norfolk Place, London W2 1PG, UK. Fax +44 207 594 3973. e-mail glsmith{at}ic.ac.uk
The vaccinia virus (VV) interferon (IFN)-
receptor (IFN-
R) is a 43 kDa soluble glycoprotein that is secreted from infected cells early during infection. Here we demonstrate that the IFN-
R from VV, cowpox virus and camelpox virus exists naturally as a homodimer, whereas the cellular IFN-
R dimerizes only upon binding the homodimeric IFN-
. The existence of the virus protein as a dimer in the absence of ligand may provide an advantage to the virus in efficient binding and inhibition of IFN-
in solution.
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