3it8 Citations

Crystal structure of TNFalpha complexed with a poxvirus MHC-related TNF binding protein.

Nat. Struct. Mol. Biol. 16 1189-91 (2009)
Cited: 14 times
EuropePMC logo PMID: 19838188

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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  4. A novel bat herpesvirus encodes homologues of major histocompatibility complex classes I and II, C-type lectin, and a unique family of immune-related genes. Zhang H, Todd S, Tachedjian M, Barr JA, Luo M, Yu M, Marsh GA, Crameri G, Wang LF. J. Virol. 86 8014-8030 (2012)
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  6. Structural pathways of cytokines may illuminate their roles in regulation of cancer development and immunotherapy. Guven-Maiorov E, Acuner-Ozbabacan SE, Keskin O, Gursoy A, Nussinov R. Cancers (Basel) 6 663-683 (2014)
  7. Comparative Biochemical and Functional Analysis of Viral and Human Secreted Tumor Necrosis Factor (TNF) Decoy Receptors. Pontejo SM, Alejo A, Alcami A. J. Biol. Chem. 290 15973-15984 (2015)
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