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Article

Production of soluble pMHC-I molecules in mammalian cells using the molecular chaperone TAPBPR.

Protein engineering, design & selection : PEDS - 31 Dec 2019

O'Rourke Sara M, Morozov Giora I, Roberts Jacob T, Barb Adam W, Sgourakis Nikolaos G

Abstract excerpt

Current approaches for generating major histocompatibility complex (MHC) Class-I proteins with desired bound peptides (pMHC-I) for research, diagnostic and therapeutic applications are limited by the inherent instability of empty MHC-I molecules. Using the properties of the chaperone TAP-binding protein related (TAPBPR), we have developed a robust method to produce soluble, peptide-receptive MHC-I molecules in...

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Identifiers

PMID: 32725167
DOI: 10.1093/protein/gzaa015
PMCID: PMC7451022

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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