Prominent role of secondary anchor residues in peptide binding to HLA-A2.1 molecules
Identifieur interne : 004552 ( Main/Exploration ); précédent : 004551; suivant : 004553Prominent role of secondary anchor residues in peptide binding to HLA-A2.1 molecules
Auteurs : Jörg Ruppert [États-Unis] ; John Sidney [États-Unis] ; Esteban Celis [États-Unis] ; Ralph T. Kubo [États-Unis] ; Howard M. Grey [États-Unis] ; Alessandro Sette [États-Unis]Source :
- Cell [ 0092-8674 ] ; 1993.
English descriptors
- Teeft :
- Affinity, Amino, Amino acid, Amino acid group, Amino acid residues, Amino acid substitutions, Amino acids, Analog, Anchor positions, Anchor residues, Aromatic residues, Assay, Basic residues, Binder, Binding, Binding affinity, Binding assays, Binding capacity, Canonical, Canonical anchor residues, Canonical anchors, Cell responses, Certain residue, Conservative substitutions, Deleterious residues, Detectable binding, Detrimental effects, Extra electron density, Falk, Frequency ratios, Good agreement, Good binding, High affinity, High affinity binders, High affinity binding, Histocompatibility, Immunol, Independent experiments, Inhibitory, Inhibitory concentration, Inhibitory dose, Intermediate affinity, Intermediate binders, Large numbers, Lower affinity, Mage, Main anchor residues, Main anchors, Major histocompatibility, Model peptide, Molecule, More unfavored residues, Negative binders, Negative charges, Negative effects, Nonanchor, Nonanchor positions, Nonanchor residues, Nonbinders, Nonbinding peptides, Parham, Peptide, Peptide antigens, Peptide binding, Peptide binding groove, Peptide ligands, Peptides binding, Peptides peptides, Poor binding, Preferred residues, Protein sequences, Quantitative assay, Residue, Saper, Secondary anchor residues, Secondary anchors, Secondary effects, Secondary pockets, Self peptides, Sette, Side chains, Simple peptides, Standard peptide, Structural requirements, Substitution, Synthetic peptides, Tumor origin, Unfavored, Unfavored residue, Unfavored residues, Viral, Weak binders.
Abstract
Abstract: The functional determinants of histocompatibility leukocyte antigen (HLA)-A2.1-peptide interactions have been detailed by the use of quantitative molecular binding assays and a chemically synthesized library of naturally occurring epitopes. The importance of hydrophobic anchor residues in position 2 and the C-terminus was confirmed. These anchors are necessary, but not sufficient, for high affinity binding, as the predictions based solely on these anchors are only about 30% accurate. Prominent roles for several other positions (1, 3, and 7) were also demonstrated. The location of these residues within the peptides matches secondary A2.1 pockets previously demonstrated by X-ray crystallography. From a functional standpoint, similar dominant negative effects on binding were observed for charged residues in both nonamers and decamers, while positive effects differed between nonamers and decamers. An extended motif taking into account secondary anchors increased the predictability of A2.1-binding epitopes to a level of 70%, underscoring the practical usefulness of extended motifs.
Url:
DOI: 10.1016/0092-8674(93)90472-3
Affiliations:
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Le document en format XML
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<term>Amino</term>
<term>Amino acid</term>
<term>Amino acid group</term>
<term>Amino acid residues</term>
<term>Amino acid substitutions</term>
<term>Amino acids</term>
<term>Analog</term>
<term>Anchor positions</term>
<term>Anchor residues</term>
<term>Aromatic residues</term>
<term>Assay</term>
<term>Basic residues</term>
<term>Binder</term>
<term>Binding</term>
<term>Binding affinity</term>
<term>Binding assays</term>
<term>Binding capacity</term>
<term>Canonical</term>
<term>Canonical anchor residues</term>
<term>Canonical anchors</term>
<term>Cell responses</term>
<term>Certain residue</term>
<term>Conservative substitutions</term>
<term>Deleterious residues</term>
<term>Detectable binding</term>
<term>Detrimental effects</term>
<term>Extra electron density</term>
<term>Falk</term>
<term>Frequency ratios</term>
<term>Good agreement</term>
<term>Good binding</term>
<term>High affinity</term>
<term>High affinity binders</term>
<term>High affinity binding</term>
<term>Histocompatibility</term>
<term>Immunol</term>
<term>Independent experiments</term>
<term>Inhibitory</term>
<term>Inhibitory concentration</term>
<term>Inhibitory dose</term>
<term>Intermediate affinity</term>
<term>Intermediate binders</term>
<term>Large numbers</term>
<term>Lower affinity</term>
<term>Mage</term>
<term>Main anchor residues</term>
<term>Main anchors</term>
<term>Major histocompatibility</term>
<term>Model peptide</term>
<term>Molecule</term>
<term>More unfavored residues</term>
<term>Negative binders</term>
<term>Negative charges</term>
<term>Negative effects</term>
<term>Nonanchor</term>
<term>Nonanchor positions</term>
<term>Nonanchor residues</term>
<term>Nonbinders</term>
<term>Nonbinding peptides</term>
<term>Parham</term>
<term>Peptide</term>
<term>Peptide antigens</term>
<term>Peptide binding</term>
<term>Peptide binding groove</term>
<term>Peptide ligands</term>
<term>Peptides binding</term>
<term>Peptides peptides</term>
<term>Poor binding</term>
<term>Preferred residues</term>
<term>Protein sequences</term>
<term>Quantitative assay</term>
<term>Residue</term>
<term>Saper</term>
<term>Secondary anchor residues</term>
<term>Secondary anchors</term>
<term>Secondary effects</term>
<term>Secondary pockets</term>
<term>Self peptides</term>
<term>Sette</term>
<term>Side chains</term>
<term>Simple peptides</term>
<term>Standard peptide</term>
<term>Structural requirements</term>
<term>Substitution</term>
<term>Synthetic peptides</term>
<term>Tumor origin</term>
<term>Unfavored</term>
<term>Unfavored residue</term>
<term>Unfavored residues</term>
<term>Viral</term>
<term>Weak binders</term>
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<front><div type="abstract" xml:lang="en">Abstract: The functional determinants of histocompatibility leukocyte antigen (HLA)-A2.1-peptide interactions have been detailed by the use of quantitative molecular binding assays and a chemically synthesized library of naturally occurring epitopes. The importance of hydrophobic anchor residues in position 2 and the C-terminus was confirmed. These anchors are necessary, but not sufficient, for high affinity binding, as the predictions based solely on these anchors are only about 30% accurate. Prominent roles for several other positions (1, 3, and 7) were also demonstrated. The location of these residues within the peptides matches secondary A2.1 pockets previously demonstrated by X-ray crystallography. From a functional standpoint, similar dominant negative effects on binding were observed for charged residues in both nonamers and decamers, while positive effects differed between nonamers and decamers. An extended motif taking into account secondary anchors increased the predictability of A2.1-binding epitopes to a level of 70%, underscoring the practical usefulness of extended motifs.</div>
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<name sortKey="Kubo, Ralph T" sort="Kubo, Ralph T" uniqKey="Kubo R" first="Ralph T." last="Kubo">Ralph T. Kubo</name>
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<name sortKey="Sidney, John" sort="Sidney, John" uniqKey="Sidney J" first="John" last="Sidney">John Sidney</name>
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