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

HLA-DQB1 codon 57 is critical for peptide binding and recognition.

The Journal of experimental medicine - 1 Mar 1996

Kwok W W, Domeier M E, Johnson M L, Nepom G T, Koelle D M

Abstract excerpt

The association of specific HLA-DQ alleles with autoimmunity is correlated with discrete polymorphisms in the HLA-DQ sequence that are localized within sites suitable for peptide recognition. The polymorphism at residue 57 of the DQB1 polypeptide is of particular interest since it may play a major structural role in the formation of a salt bridge structure at one end of the peptide-binding cleft of the DQ...

Read the complete abstract on PubMed

Topics

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

Share to Alleles
Share to Amino Acid Sequence
Share to B-Lymphocytes

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

Share to Binding Sites

Share to Biological Evolution

Share to Lymphocyte Activation

Share to Molecular Sequence Data

Source

Open in PubMed Open full text

Identifiers

PMID: 8642268
DOI: 10.1084/jem.183.3.1253
PMCID: PMC2192334

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

HLA-DQB1 codon 57 is critical for peptide binding and recognition.PMID 8642268Read ↗

Critical contribution of beta chain residue 57 in peptide binding ability of both HLA-DR and -DQ molecules.Semantic proximity Read ↗

A new model defines the minimal set of polymorphism in HLA-DQ and -DR that determines susceptibility and resistance to autoimmune diabetes.Semantic proximity Read ↗

The diabetogenic mouse MHC class II molecule I-Ag7 is endowed with a switch that modulates TCR affinity.Semantic proximity Read ↗

Additive and interaction effects at three amino acid positions in HLA-DQ and HLA-DR molecules drive type 1 diabetes risk.Semantic proximity Read ↗

Allele-specific motifs characterize HLA-DQ interactions with a diabetes-associated peptide derived from glutamic acid decarboxylase.Semantic proximity Read ↗

DQB1*0202 and the new DQB1*0203 allele: a fourth pair of DQB1 alleles differing only at codon 57.Semantic proximity Read ↗

Structural basis of specificity and degeneracy of T cell recognition: pluriallelic restriction of T cell responses to a peptide antigen involves both specific and promiscuous interactions between the T cell receptor, peptide, and HLA-DR.Semantic proximity Read ↗

HLA-DQ polymorphisms are highly selective for peptide binding interactions.Semantic proximity Read ↗

Shared molecular amino acid signature in the HLA-DR peptide binding pocket predisposes to both autoimmune diabetes and thyroiditis.Semantic proximity Read ↗

The Cys-67 residue of HLA-B27 influences cell surface stability, peptide specificity, and T-cell antigen presentation.Semantic proximity Read ↗

Residues in HLA class I that Account for Variation of the HIV Host Response Distinctly Modulate Interactions with TCR and KIRsSemantic proximity Read ↗

The P9 pocket of HLA-DQ2 (non-Aspbeta57) has no particular preference for negatively charged anchor residues found in other type 1 diabetes-predisposing non-Aspbeta57 MHC class II molecules.Semantic proximity Read ↗

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