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@ARTICLE{Fisette:889726,
      author       = {Fisette, Olivier and Schröder, Gunnar F. and Schäfer,
                      Lars V.},
      title        = {{A}tomistic structure and dynamics of the human {MHC}-{I}
                      peptide-loading complex},
      journal      = {Proceedings of the National Academy of Sciences of the
                      United States of America},
      volume       = {117},
      number       = {34},
      issn         = {1091-6490},
      address      = {Washington, DC},
      publisher    = {National Acad. of Sciences},
      reportid     = {FZJ-2021-00347},
      pages        = {20597 - 20606},
      year         = {2020},
      abstract     = {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.},
      cin          = {IBI-7},
      ddc          = {500},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551)},
      pid          = {G:(DE-HGF)POF3-551},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {32788370},
      UT           = {WOS:000572978200009},
      doi          = {10.1073/pnas.2004445117},
      url          = {https://juser.fz-juelich.de/record/889726},
}