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The vaccinia virus (VV) interferon (IFN)-γ receptor (IFN-γR) is a 43 kDa soluble glycoprotein that is secreted from infected cells early during infection. Here we demonstrate that the IFN-γR from VV, cowpox virus and camelpox virus exists naturally as a homodimer, whereas the cellular IFN-γR dimerizes only upon binding the homodimeric IFN-γ. 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-γ in solution.

Original publication

DOI

10.1099/0022-1317-83-3-545

Type

Journal article

Journal

Journal of General Virology

Publisher

Microbiology Society

Publication Date

01/03/2002

Volume

83

Pages

545 - 549