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TitleERAP1 enzyme-mediated trimming and structural analyses of MHC I-bound precursor peptides yield novel insights into antigen processing and presentation.
Journal, issue, pagesJ. Biol. Chem., Vol. 294, Page 18534-18544, Year 2019
Publish dateMay 20, 2019 (structure data deposition date)
AuthorsLi, L. / Batliwala, M. / Bouvier, M.
External linksJ. Biol. Chem. / PubMed:31601650
MethodsX-ray diffraction
Resolution1.396 - 1.65 Å
Structure data

PDB-6p23:
Structure of a nested set of N-terminally extended MHC I-peptides provide novel insights into antigen processing presentation
Method: X-RAY DIFFRACTION / Resolution: 1.595 Å

PDB-6p27:
Structure of a nested set of N-terminally extended MHC I-peptides provides novel insights into antigen processing and presentation
Method: X-RAY DIFFRACTION / Resolution: 1.593 Å

PDB-6p2c:
Structure of a nested set of N-terminally extended MHC I-peptides provides novel insights into antigen processing and presentation
Method: X-RAY DIFFRACTION / Resolution: 1.396 Å

PDB-6p2f:
Structure of a nested set of N-terminally extended MHC I-peptides provides novel insights into antigen processing and presentation
Method: X-RAY DIFFRACTION / Resolution: 1.482 Å

PDB-6p2s:
Structure of a nested set of N-terminally extended MHC I-peptides provide novel insights into antigen processing and presentation
Method: X-RAY DIFFRACTION / Resolution: 1.65 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
  • human immunodeficiency virus 1
KeywordsIMMUNE SYSTEM / MHC I antigen processing / MHC I antigen presentation / MHC I structure / MHC I immunopeptide

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