How conformational changes near the F pocket of MHC class I proteins mediate chaperone assisted peptide loading.

ABSTRACT:

Background

Efficient recognition of antigenic peptides bound to major histocompatibility complex (MHC) class I molecules on the surface of cells by immune cells requires sufficiently stable peptide-MHC I complexes. Antigenic peptides of 8-10 amino acids are typically bound in a narrow cleft between two flanking α₁ and α₂ helices on top of an extended β sheet floor. For some MHC I alleles the efficient loading with high-affinity peptides in the endoplasmic reticulum (ER) requires the transient binding and assistance of the chaperone proteins tapasin and/or TAPBPR. The structures of both chaperones in complex with MHC I molecules have been resolved and indicate similar structural interface elements and also similar structural changes of the bound MHC I molecules

SUBMITTER: Goppert S 

PROVIDER: S-EPMC12745280 | biostudies-literature | 2025

REPOSITORIES: biostudies-literature