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- W2321810726 abstract "Major Histocompatibility complex (MHC) class I proteins bind peptides of eight to ten amino acids to present them at the cell surface to cytotoxic T cells. The class I binding groove binds the peptide via hydrogen bonds with the peptide termini and via diverse interactions with the anchor residue side chains of the peptide. To elucidate which of these interactions is most important for the thermodynamic and kinetic stability of the peptide-bound state, we have combined molecular dynamics simulations and experimental approaches in an investigation of the conformational dynamics and binding parameters of class I molecules with optimal and truncated natural peptide epitopes. We show that the F pocket region dominates the conformational and thermodynamic properties of the binding groove, and that therefore the binding of the C terminus of the peptide to the F pocket region plays a crucial role in bringing about the peptide-bound state of MHC class I." @default.
- W2321810726 created "2016-06-24" @default.
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- W2321810726 date "2015-01-01" @default.
- W2321810726 modified "2023-10-02" @default.
- W2321810726 title "The Carboxy Terminus of the Ligand Peptide Determines MHC Class I Complex Stability: A Combined Molecular Dynamics and Experimental Study" @default.
- W2321810726 doi "https://doi.org/10.1016/j.bpj.2014.11.1716" @default.
- W2321810726 hasPublicationYear "2015" @default.
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