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Dipeptides promote folding and peptide binding of MHC class I molecules
by
Ramnarayan, Venkat Raman
, Schuster, Heiko
, Zacharias, Martin
, Saini, Sunil Kumar
, Ostermeir, Katja
, Springer, Sebastian
in
Amino acids
/ Amino Acids - metabolism
/ Anisotropy
/ Binding energy
/ Biological Sciences
/ Cells
/ Crystal structure
/ Cytometry
/ dipeptides
/ Dipeptides - genetics
/ Dipeptides - metabolism
/ Endoplasmic Reticulum - metabolism
/ Escherichia coli
/ Flow Cytometry
/ Fluorescence
/ Fluorescence Polarization
/ HLA-A2 Antigen - metabolism
/ Humans
/ Hydrophobic and Hydrophilic Interactions
/ hydrophobicity
/ Ligands
/ Microscopy, Fluorescence
/ Molecular Dynamics Simulation
/ Molecules
/ Peptides
/ Protein Binding
/ Protein Conformation
/ Protein Folding
/ Proteins
/ T lymphocytes
2013
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Dipeptides promote folding and peptide binding of MHC class I molecules
by
Ramnarayan, Venkat Raman
, Schuster, Heiko
, Zacharias, Martin
, Saini, Sunil Kumar
, Ostermeir, Katja
, Springer, Sebastian
in
Amino acids
/ Amino Acids - metabolism
/ Anisotropy
/ Binding energy
/ Biological Sciences
/ Cells
/ Crystal structure
/ Cytometry
/ dipeptides
/ Dipeptides - genetics
/ Dipeptides - metabolism
/ Endoplasmic Reticulum - metabolism
/ Escherichia coli
/ Flow Cytometry
/ Fluorescence
/ Fluorescence Polarization
/ HLA-A2 Antigen - metabolism
/ Humans
/ Hydrophobic and Hydrophilic Interactions
/ hydrophobicity
/ Ligands
/ Microscopy, Fluorescence
/ Molecular Dynamics Simulation
/ Molecules
/ Peptides
/ Protein Binding
/ Protein Conformation
/ Protein Folding
/ Proteins
/ T lymphocytes
2013
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Dipeptides promote folding and peptide binding of MHC class I molecules
by
Ramnarayan, Venkat Raman
, Schuster, Heiko
, Zacharias, Martin
, Saini, Sunil Kumar
, Ostermeir, Katja
, Springer, Sebastian
in
Amino acids
/ Amino Acids - metabolism
/ Anisotropy
/ Binding energy
/ Biological Sciences
/ Cells
/ Crystal structure
/ Cytometry
/ dipeptides
/ Dipeptides - genetics
/ Dipeptides - metabolism
/ Endoplasmic Reticulum - metabolism
/ Escherichia coli
/ Flow Cytometry
/ Fluorescence
/ Fluorescence Polarization
/ HLA-A2 Antigen - metabolism
/ Humans
/ Hydrophobic and Hydrophilic Interactions
/ hydrophobicity
/ Ligands
/ Microscopy, Fluorescence
/ Molecular Dynamics Simulation
/ Molecules
/ Peptides
/ Protein Binding
/ Protein Conformation
/ Protein Folding
/ Proteins
/ T lymphocytes
2013
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Dipeptides promote folding and peptide binding of MHC class I molecules
Journal Article
Dipeptides promote folding and peptide binding of MHC class I molecules
2013
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Overview
MHC class I molecules bind only those peptides with high affinity that conform to stringent length and sequence requirements. We have now investigated which peptides can aid the in vitro folding of class I molecules, and we find that the dipeptide glycyl-leucine efficiently supports the folding of HLA-A*02:01 and H-2K ᵇ into a peptide-receptive conformation that rapidly binds high-affinity peptides. Treatment of cells with glycyl-leucine induces accumulation of peptide-receptive H-2K ᵇ and HLA-A*02:01 at the surface of cells. Other dipeptides with a hydrophobic second amino acid show similar enhancement effects. Our data suggest that the dipeptides bind into the F pocket like the C-terminal amino acids of a high-affinity peptide.
Publisher
National Academy of Sciences,National Acad Sciences
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