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Structure paper

TitleCrystal structure of a TAPBPR-MHC I complex reveals the mechanism of peptide editing in antigen presentation.
Journal, issue, pagesScience, Vol. 358, Page 1064-1068, Year 2017
Publish dateJul 10, 2017 (structure data deposition date)
AuthorsJiang, J. / Natarajan, K. / Boyd, L.F. / Morozov, G.I. / Mage, M.G. / Margulies, D.H.
External linksScience / PubMed:29025991
MethodsX-ray diffraction
Resolution1.584 - 3.412 Å
Structure data

PDB-5wer:
Crystal Structure of TAPBPR and H2-Dd complex
Method: X-RAY DIFFRACTION / Resolution: 3.412 Å

PDB-5wes:
Crystal Structure H2-Dd with disulfide-linked 5mer peptide
Method: X-RAY DIFFRACTION / Resolution: 2.706 Å

PDB-5wet:
Crystal Structure of H2-Dd with disulfide-linked 6mer peptide
Method: X-RAY DIFFRACTION / Resolution: 2.64 Å

PDB-5weu:
Crystal Structure of H2-Dd with disulfide-linked 10mer peptide
Method: X-RAY DIFFRACTION / Resolution: 1.584 Å

Chemicals

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-GOL:
GLYCEROL

ChemComp-1PE:
PENTAETHYLENE GLYCOL / precipitant*YM

ChemComp-CIT:
CITRIC ACID

ChemComp-GLY:
GLYCINE

ChemComp-LEU:
LEUCINE

ChemComp-HOH:
WATER

Source
  • mus musculus (house mouse)
  • homo sapiens (human)
  • human immunodeficiency virus type 1 group m subtype b
KeywordsIMMUNE SYSTEM / Antigen presentation / peptide editing / MAJOR HISTOMPATIBILITY COMPLEX CLASS I / MHC-I / TAPASIN / Peptide Loading Complex / PLC / IMMUNE RESPONSE / TAPBPR / H2-Dd / H-2DD

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