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  Assembly of the MHC I peptideloading complex determined by a conserved ionic lock-switch

Blees, A., Reichel, K., Trowitzsch, S., Fisette, O., Bock, C., Abele, R., et al. (2015). Assembly of the MHC I peptideloading complex determined by a conserved ionic lock-switch. Scientific Reports, 5: 17341. doi:10.1038/srep17341 1.

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 Creators:
Blees, Andreas1, Author
Reichel, Katrin2, 3, Author              
Trowitzsch, Simon1, Author
Fisette, Olivier2, Author
Bock, Christoph1, Author
Abele, Rupert1, Author
Hummer, Gerhard3, Author              
Schäfer, Lars V.2, Author
Tampé, Robert1, 4, Author
Affiliations:
1Institute of Biochemistry, Biocenter, Goethe-University Frankfurt am Main, Max-von-Laue-Str. 9, D-60438 Frankfurt am Main, Germany, ou_persistent22              
2Lehrstuhl für Theoretische Chemie, Ruhr-University Bochum, D-44780 Bochum, Germany, ou_persistent22              
3Department of Theoretical Biophysics, Max Planck Institute of Biophysics, Max Planck Society, ou_2068292              
4Cluster of Excellence–Macromolecular Complexes, Goethe-University Frankfurt am Main, Max-von-Laue-Str. 9, 60438 Frankfurt am Main, Germany, ou_persistent22              

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 Abstract: Salt bridges in lipid bilayers play a decisive role in the dynamic assembly and downstream signaling of the natural killer and T-cell receptors. Here, we describe the identification of an inter-subunit salt bridge in the membrane within yet another key component of the immune system, the peptide-loading complex (PLC). The PLC regulates cell surface presentation of self-antigens and antigenic peptides via molecules of the major histocompatibility complex class I. We demonstrate that a single salt bridge in the membrane between the transporter associated with antigen processing TAP and the MHC I-specific chaperone tapasin is essential for the assembly of the PLC and for efficient MHC I antigen presentation. Molecular modeling and all-atom molecular dynamics simulations suggest an ionic lock-switch mechanism for the binding of TAP to tapasin, in which an unfavorable uncompensated charge in the ER-membrane is prevented through complex formation. Our findings not only deepen the understanding of the interaction network within the PLC, but also provide evidence for a general interaction principle of dynamic multiprotein membrane complexes in immunity.

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Language(s): eng - English
 Dates: 2015-08-132015-10-152015-11-27
 Publication Status: Published online
 Pages: 11
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1038/srep17341 1
 Degree: -

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Title: Scientific Reports
  Abbreviation : Sci. Rep.
Source Genre: Journal
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Publ. Info: London, UK : Nature Publishing Group
Pages: - Volume / Issue: 5 Sequence Number: 17341 Start / End Page: - Identifier: Other: 2045-2322
CoNE: https://pure.mpg.de/cone/journals/resource/2045-2322