3IT8
Crystal structure of TNF alpha complexed with a poxvirus MHC-related TNF binding protein
Summary for 3IT8
Entry DOI | 10.2210/pdb3it8/pdb |
Descriptor | Tumor necrosis factor, 2L protein, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total) |
Functional Keywords | mhc class i homolog, cell membrane, cytokine, disulfide bond, glycoprotein, lipoprotein, membrane, myristate, phosphoprotein, secreted, signal-anchor, transmembrane, immune system |
Biological source | Homo sapiens (human) More |
Total number of polymer chains | 12 |
Total formula weight | 335667.46 |
Authors | Yang, Z.,West Jr., A.P.,Bjorkman, P.J. (deposition date: 2009-08-27, release date: 2009-10-20, Last modification date: 2024-11-06) |
Primary citation | Yang, Z.,West, A.P.,Bjorkman, P.J. Crystal structure of TNFalpha complexed with a poxvirus MHC-related TNF binding protein Nat.Struct.Mol.Biol., 16:1189-1191, 2009 Cited by PubMed 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. PubMed: 19838188DOI: 10.1038/nsmb.1683 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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