Crystal structure of TNFalpha complexed with a poxvirus MHC-related TNF binding protein.
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.
Yang
Zhiru
Z
Division of Biology 114-96, California Institute of Technology, Pasadena, California, USA.
West
Anthony P
AP
Bjorkman
Pamela J
PJ
D001665:Binding Sites; D015395:Histocompatibility Antigens Class I / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D008958:Models, Molecular; D011212:Poxviridae / Q000378:metabolism*; D011485:Protein Binding; D017433:Protein Structure, Secondary; D014409:Tumor Necrosis Factor-alpha / Q000737:chemistry* / Q000378:metabolism*; D014764:Viral Proteins / Q000737:chemistry* / Q000378:metabolism*
D015395:Histocompatibility Antigens Class I; D014409:Tumor Necrosis Factor-alpha; D014764:Viral Proteins