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Structure paper

TitleTAPBPR employs a ligand-independent docking mechanism to chaperone MR1 molecules.
Journal, issue, pagesNat. Chem. Biol., Vol. 18, Page 859-868, Year 2022
Publish dateJul 29, 2021 (structure data deposition date)
AuthorsMcShan, A.C. / Devlin, C.A. / Papadaki, G.F. / Sun, Y. / Green, A.I. / Morozov, G.I. / Burslem, G.M. / Procko, E. / Sgourakis, N.G.
External linksNat. Chem. Biol. / PubMed:35725941
MethodsNMR (solution)
Structure data

PDB-7rno:
Model of the Ac-6-FP/hpMR1/bB2m/TAPBPR complex from integrated docking, NMR and restrained MD
Method: SOLUTION NMR

Chemicals

ChemComp-30W:
N-(6-formyl-4-oxo-3,4-dihydropteridin-2-yl)acetamide

Source
  • homo sapiens (human)
  • bos taurus (domestic cattle)
KeywordsIMMUNE SYSTEM / TAPBPR / MR1 / MHC-I / chaperones / adaptive immune system / antigen processing and presentation

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