Cargando…
Assembly of the MHC I peptide-loading complex determined by a conserved ionic lock-switch
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-loa...
Autores principales: | Blees, Andreas, Reichel, Katrin, Trowitzsch, Simon, Fisette, Olivier, Bock, Christoph, Abele, Rupert, Hummer, Gerhard, Schäfer, Lars V., Tampé, Robert |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2015
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4661472/ https://www.ncbi.nlm.nih.gov/pubmed/26611325 http://dx.doi.org/10.1038/srep17341 |
Ejemplares similares
-
Structural and functional insights into the interaction and targeting hub TMD0 of the polypeptide transporter TAPL
por: Bock, Christoph, et al.
Publicado: (2018) -
Molecular mechanism of peptide editing in the tapasin–MHC I complex
por: Fisette, Olivier, et al.
Publicado: (2016) -
Direct evidence that the N-terminal extensions of the TAP complex act as autonomous interaction scaffolds for the assembly of the MHC I peptide-loading complex
por: Hulpke, Sabine, et al.
Publicado: (2012) -
Dynamic interactome of the MHC I peptide loading complex in human dendritic cells
por: Barends, Martina, et al.
Publicado: (2023) -
Molecular basis of MHC I quality control in the peptide loading complex
por: Domnick, Alexander, et al.
Publicado: (2022)