Crystal structure of TNFalpha complexed with a poxvirus MHC-related TNF binding protein
Zhiru Yang1, Anthony P West, Pamela J Bjorkman
1Division of Biology 114-96, California Institute of Technology, Pasadena, California, USA.
Abstract:
The poxvirus 2L protein binds tumor necrosis factor-alpha (TNFalpha) to inhibit host antiviral and immune responses. The 2.8-A 2L-TNFalpha structure reveals three symmetrically arranged 2L molecules per TNFalpha trimer. 2L resembles class I major histocompatibility complex (MHC) molecules but lacks a peptide-binding groove and beta2-microglobulin light chain. Overlap between the 2L and host TNF receptor-binding sites on TNFalpha rationalizes 2L inhibition of TNFalpha-TNF receptor interactions and prevention of TNFalpha-induced immune responses.
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