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TitleThe high resolution structures of highly bulged viral epitopes bound to the major histocompatability class I: Implications for T-cell receptor engagement and T-cell immunodominance
Journal, issue, pagesJ. Biol. Chem., Vol. 280, Page 23900-23909, Year 2005
Publish dateApr 26, 2005 (structure data deposition date)
AuthorsTynan, F.E. / Borg, N.A. / Miles, J.J. / Beddoe, T. / El-Hassen, D. / Silins, S.L. / van Zuylen, W.J. / Purcell, A.W. / Kjer-Nielsen, L. / McCluskey, J. ...Tynan, F.E. / Borg, N.A. / Miles, J.J. / Beddoe, T. / El-Hassen, D. / Silins, S.L. / van Zuylen, W.J. / Purcell, A.W. / Kjer-Nielsen, L. / McCluskey, J. / Burrows, S.R. / Rossjohn, J.
External linksJ. Biol. Chem. / PubMed:15849183
MethodsX-ray diffraction
Resolution1.5 - 1.6 Å
Structure data

PDB-1zhk:
Crystal structure of HLA-B*3501 presenting 13-mer EBV antigen LPEPLPQGQLTAY
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

PDB-1zhl:
Crystal structure of HLA-B*3508 presenting 13-mer EBV antigen LPEPLPQGQLTAY
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsIMMUNE SYSTEM / T-cell receptor / bulged epitopes

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