Hauptseite > Publikationsdatenbank > Atomistic structure and dynamics of the human MHC-I peptide-loading complex > print

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024 7 _ |a 10.1073/pnas.2004445117
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037 _ _ |a FZJ-2021-00347
082 _ _ |a 500
100 1 _ |a Fisette, Olivier
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245 _ _ |a Atomistic structure and dynamics of the human MHC-I peptide-loading complex
260 _ _ |a Washington, DC
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520 _ _ |a The major histocompatibility complex class-I (MHC-I) peptide-loading complex (PLC) is a cornerstone of the human adaptive immune system, being responsible for processing antigens that allow killer T cells to distinguish between healthy and compromised cells. Based on a recent low-resolution cryo-electron microscopy (cryo-EM) structure of this large membrane-bound protein complex, we report an atomistic model of the PLC and study its conformational dynamics on the multimicrosecond time scale using all-atom molecular dynamics (MD) simulations in an explicit lipid bilayer and water environment (1.6 million atoms in total). The PLC has a layered structure, with two editing modules forming a flexible protein belt surrounding a stable, catalytically active core. Tapasin plays a central role in the PLC, stabilizing the MHC-I binding groove in a conformation reminiscent of antigen-loaded MHC-I. The MHC-I–linked glycan steers a tapasin loop involved in peptide editing toward the binding groove. Tapasin conformational dynamics are also affected by calreticulin through a conformational selection mechanism that facilitates MHC-I recruitment into the complex.
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700 1 _ |a Schröder, Gunnar F.
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700 1 _ |a Schäfer, Lars V.
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773 _ _ |a 10.1073/pnas.2004445117
|g Vol. 117, no. 34, p. 20597 - 20606
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|t Proceedings of the National Academy of Sciences of the United States of America
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856 4 _ |y Published on 2020-08-11. Available in OpenAccess from 2021-02-11.
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