Conformational flexibility of a free and TCR-bound pMHC-I protein investigated by long-term molecular dynamics simulations.

ABSTRACT:

Background

Major histocompatibility complexes (MHCs) play a crucial role in the cell-mediated adaptive immune response as they present antigenic peptides (p) which are recognized by host T cells through a complex formation of the T cell receptor (TCR) with pMHC. In the present study, we report on changes in conformational flexibility within a pMHC molecule upon TCR binding by looking at molecular dynamics (MD) simulations of the free and the TCR-bound pMHC-I protein of the LC13-HLA-B*44:05-pEEYLQAFTY complex.

Results

We performed long-term MD simulations with a total simulation time of 8 µs, employing 10 independent 400 ns replicas for the free and the TCR-bound pMHC system. Upon TCR ligation, we observed a reduced dynamic flexibility in the central residues of the peptide a

SUBMITTER: Tomasiak L 

PROVIDER: S-EPMC9335952 | biostudies-literature | 2022 Jul

REPOSITORIES: biostudies-literature