Science · 1994 · 298 citations · 37 references
Life SciencesBiochemistryImmunologyMolecular ImmunologyMolecular RecognitionProtein FoldingAntigen PresentationHuman Leukocyte Antigen SystemMajor Histocompatibility ComplexPeptide ChemistryProtein Folding ThermodynamicsProtein StructureAmino AcidsClass I Histocompatibility AntigensHla Class I MoleculesMajor Histocompatibility Complex Class I RecognitionMhc Class I MoleculesPeptide FoldingPeptide-mhc StabilityThermal Stability
An influenza virus matrix peptide in which either the charged amino or carboxyl terminus was substituted by methyl groups promoted folding of the class I human histocompatibility antigen (HLA-A2). A peptide modified at both termini did not promote stable folding. The thermal stability of HLA-A2 complexed with peptides that did not have either terminus was approximately 22 degrees C lower than that of the control peptide, whereas matrix peptide in which both anchor positions were substituted by alanines had its stability decreased by only 5.5 degrees C. Thus, the conserved major histocompatibility complex class I residues at both ends of the peptide binding site form energetically important sites for binding the termini of short peptides.
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Structure of the human class I histocompatibility antigen, HLA-A2
Pamela J. Björkman, Mark A. Saper, Boudjéma Samraoui et al. · Nature · 1987 · 3.5K citations
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