4E5X
Crystal structure of a complex between the human adenovirus type 2 E3-19K protein and MHC class I molecule HLA-A2/Tax
Summary for 4E5X
Entry DOI | 10.2210/pdb4e5x/pdb |
Descriptor | HLA class I histocompatibility antigen, A-2 alpha chain, Beta-2-microglobulin, Protein Tax-1, ... (5 entities in total) |
Functional Keywords | ad2 e3-19k-hla-a2 complex, unique tertiary structure, adenovirus e3-19k, immune evasion function, mhc class i molecule, endoplasmic reticulum, immune system-transcription complex, immune system/transcription |
Biological source | Homo sapiens (human) More |
Cellular location | Membrane; Single-pass type I membrane protein: P01892 Secreted: P61769 Host nucleus (By similarity): P0C213 Host endoplasmic reticulum membrane; Single- pass type I membrane protein: P68979 |
Total number of polymer chains | 8 |
Total formula weight | 113485.32 |
Authors | Li, L.,Bouvier, M. (deposition date: 2012-03-14, release date: 2012-10-10, Last modification date: 2024-11-27) |
Primary citation | Li, L.,Muzahim, Y.,Bouvier, M. Crystal structure of adenovirus E3-19K bound to HLA-A2 reveals mechanism for immunomodulation. Nat.Struct.Mol.Biol., 19:1176-1181, 2012 Cited by PubMed Abstract: E3-19K binds to and retains MHC class I molecules in the endoplasmic reticulum, suppressing anti-adenovirus activities of T cells. We determined the structure of the adenovirus serotype 2 (Ad2, species C) E3-19K-HLA-A2 complex to 1.95-Å resolution. Ad2 E3-19K binds to the N terminus of the HLA-A2 groove, contacting the α1, α2 and α3 domains and β(2)m. Ad2 E3-19K has a unique structure comprising a large N-terminal domain, formed by two partially overlapping β-sheets arranged in a V shape, and a C-terminal α-helix and tail. The structure reveals determinants in E3-19K and HLA-A2 that are important for complex formation; conservation of some of these determinants in E3-19K proteins of different species and MHC I molecules of different loci suggests a universal binding mode for all E3-19K proteins. Our structure is important for understanding the immunomodulatory function of E3-19K. PubMed: 23042604DOI: 10.1038/nsmb.2396 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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