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Structure paper

TitleUnexpected T-cell recognition of an altered peptide ligand is driven by reversed thermodynamics.
Journal, issue, pagesEur. J. Immunol., Vol. 42, Page 2990-3000, Year 2012
Publish dateFeb 24, 2011 (structure data deposition date)
AuthorsAllerbring, E.B. / Duru, A.D. / Uchtenhagen, H. / Madhurantakam, C. / Tomek, M.B. / Grimm, S. / Mazumdar, P.A. / Friemann, R. / Uhlin, M. / Sandalova, T. ...Allerbring, E.B. / Duru, A.D. / Uchtenhagen, H. / Madhurantakam, C. / Tomek, M.B. / Grimm, S. / Mazumdar, P.A. / Friemann, R. / Uhlin, M. / Sandalova, T. / Nygren, P.A. / Achour, A.
External linksEur. J. Immunol. / PubMed:22837158
MethodsX-ray diffraction
Resolution2 - 2.41 Å
Structure data

PDB-3quk:
Crystal structures of the murine class I major histocompatibility complex H-2Db in complex with LCMV-derived gp33 altered peptide ligand (Y4A)
Method: X-RAY DIFFRACTION / Resolution: 2.41 Å

PDB-3qul:
Crystal structures of the murine class I major histocompatibility complex H-2Db in complex with LCMV-derived gp33 altered peptide ligand (Y4S)
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • mus musculus (house mouse)
  • lymphocytic choriomeningitis virus
KeywordsIMMUNE SYSTEM / Murine MHC / LCMV / receptor binding / beta2-microglobulin / T cell recognition / T cell receptor / cell surface

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