Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Implication of HLA-DR residues at positions 67, 71, and 86 in interaction between HLA-DR11 and peptide HA306-320.

Journal of immunology (Baltimore, Md. : 1950) - 1 Dec 1993

Zeliszewski D, Golvano J J, Gaudebout P, Dorval I, Freidel C, Gebuhrer L, Betuel H, Borras-Cuesta F, Sterkers G

Abstract excerpt

To get further insight into the role of three polymorphic DR residues located in one alpha-helix of the HLA-DR binding groove, we studied how natural substitutions at positions 67, 71, and 86 on DR11 molecules influence MHC binding and/or T cell recognition of peptide HA306-320 and of monosubstituted peptide analogues. Our results show that: 1) Reactivities of all HA306-320-specific T cell clones tested are...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Sequence
Share to Binding Sites

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to HLA-DR Antigens

Share to Molecular Sequence Data

Share to Mutation

Share to Protein Conformation

Share to Structure-Activity Relationship

Share to T-Lymphocytes

Source

Identifiers

PMID: 7504016

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Implication of HLA-DR residues at positions 67, 71, and 86 in interaction between HLA-DR11 and peptide HA306-320.PMID 7504016Read ↗

Effect of natural polymorphism at residue 86 of the HLA-DR beta chain on peptide binding.Semantic proximity Read ↗

Individual effects of the DR11-variable beta-chain residues 67, 71, and 86 upon DR(alpha,beta 1*1101)-restricted, peptide-specific T cell proliferation.Semantic proximity Read ↗

Distant interactions between dimorphisms in HLA-DR4 radically affect recognition of defined peptides by a specific T cell clone.Semantic proximity Read ↗

Differential effect of polymorphism at HLA-DR1 beta-chain positions 85 and 86 on binding and recognition of DR1-restricted antigenic peptides.Semantic proximity Read ↗

Role of the polymorphic residues in HLA-DR molecules in allele-specific binding of peptide ligands.Semantic proximity Read ↗

Polymorphism at beta 85 and not beta 86 of HLA-DR1 is predominantly responsible for restricting the nature of the anchor side chain: implication for concerted effects of class II MHC polymorphism.Semantic proximity Read ↗

Modifying RESA protein peptide 6671 to fit into HLA-DRbeta1* pockets induces protection against malaria.Semantic proximity Read ↗

Cross-restriction of a T cell clone to HLA-DR alleles associated with rheumatoid arthritis: clues to arthritogenic peptide motifs.Semantic proximity Read ↗

Critical role for the Val/Gly86 HLA-DR beta dimorphism in autoantigen presentation to human T cells.Semantic proximity Read ↗

Analysis of allele-specific contact sites of natural HLA-DR17 ligands.Semantic proximity Read ↗

Modeling the HLA component in rheumatoid arthritis: sensitivity to DRB1 allele frequencies.Semantic proximity Read ↗

Microvariation creates significant functional differences in the DR3 molecules.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.