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Article

TAPBPR promotes antigen loading on MHC-I molecules using a peptide trap.

Nature communications - 26 May 2021

McShan Andrew C, Devlin Christine A, Morozov Giora I, Overall Sarah A, Moschidi Danai, Akella Neha, Procko Erik, Sgourakis Nikolaos G

Abstract excerpt

Chaperones Tapasin and TAP-binding protein related (TAPBPR) perform the important functions of stabilizing nascent MHC-I molecules (chaperoning) and selecting high-affinity peptides in the MHC-I groove (editing). While X-ray and cryo-EM snapshots of MHC-I in complex with TAPBPR and Tapasin, respectively, have provided important insights into the peptide-deficient MHC-I groove structure, the molecular mechanism...

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Identifiers

PMID: 34039964
DOI: 10.1038/s41467-021-23225-6
PMCID: PMC8154891

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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TAPBPR promotes antigen loading on MHC-I molecules using a peptide trap.PMID 34039964Read ↗

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