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Structure paper

TitleHLA Peptide Length Preferences Control CD8+ T Cell Responses.
Journal, issue, pagesJ. Immunol., Vol. 191, Page 561-571, Year 2013
Publish dateMar 20, 2013 (structure data deposition date)
AuthorsRist, M.J. / Theodossis, A. / Croft, N.P. / Neller, M.A. / Welland, A. / Chen, Z. / Sullivan, L.C. / Burrows, J.M. / Miles, J.J. / Brennan, R.M. ...Rist, M.J. / Theodossis, A. / Croft, N.P. / Neller, M.A. / Welland, A. / Chen, Z. / Sullivan, L.C. / Burrows, J.M. / Miles, J.J. / Brennan, R.M. / Gras, S. / Khanna, R. / Brooks, A.G. / McCluskey, J. / Purcell, A.W. / Rossjohn, J. / Burrows, S.R.
External linksJ. Immunol. / PubMed:23749632
MethodsX-ray diffraction
Resolution1.5 - 1.9 Å
Structure data

PDB-4jqv:
HLA-B*18:01 in complex with Epstein-Barr virus BZLF1-derived peptide (residues 173-180)
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

PDB-4jqx:
HLA-B*44:03 in complex with Epstein-Barr virus BZLF1-derived peptide (residues 169-180)
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-ACT:
ACETATE ION

ChemComp-HOH:
WATER

ChemComp-GOL:
GLYCEROL

Source
  • homo sapiens (human)
  • human herpesvirus 4 (Epstein-Barr virus)
KeywordsIMMUNE SYSTEM / immunoglobulin fold / antigen presentation / t-cell receptor / extracellular

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