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

Unraveling the structural basis for the unusually rich association of human leukocyte antigen DQ2.5 with class-II-associated invariant chain peptides

1 Apr 2017

Abstract excerpt

) is a class-II major histocompatibility complex protein associated with both type 1 diabetes and celiac disease. One unusual feature of DQ2.5 is its high class-II-associated invariant chain peptide (CLIP) content. Moreover, HLA-DQ2.5 preferentially binds the non-canonical CLIP2 over the canonical CLIP1. To better understand the structural basis of HLA-DQ2.5's unusual CLIP association characteristics, better...

Read the complete abstract on PubMed

Topics

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

Share to Celiac Disease Research and Management
Share to Galectins and Cancer Biology
Share to Monoclonal and Polyclonal Antibodies Research

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 28364043
DOI: 10.1074/jbc.m117.785139

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Unraveling the structural basis for the unusually rich association of human leukocyte antigen DQ2.5 with class-II-associated invariant chain peptidesPMID 28364043Read ↗

Complexes of Two Cohorts of CLIP Peptides and HLA-DQ2 of the Autoimmune DR3-DQ2 Haplotype Are Poor Substrates for HLA-DMSemantic proximity Read ↗

An insertion mutant in DQA1*0501 restores susceptibility to HLA-DM: implications for disease associations.Semantic proximity Read ↗

Large-Scale Characterization of Natural Ligands Explains the Unique Gluten-Binding Properties of HLA-DQ2Semantic proximity Read ↗

The peptide binding motif of the disease associated HLA-DQ (alpha 1* 0501, beta 1* 0201) molecule.Semantic proximity Read ↗

A general model of invariant chain association with class II major histocompatibility complex proteins.Semantic proximity Read ↗

Detailed analysis of the effects of Glu/Lys beta69 human leukocyte antigen-DP polymorphism on peptide-binding specificity.Semantic proximity Read ↗

Design, synthesis and evaluation of high-affinity binders for the celiac disease associated HLA-DQ2 molecule.Semantic proximity Read ↗

Structural basis for HLA-DQ2-mediated presentation of gluten epitopes in celiac diseaseSemantic proximity Read ↗

Molecular modeling and design of invariant chain peptides with altered dissociation kinetics from class II MHC.Semantic proximity Read ↗

Peptide binding prediction for the human class II MHC allele HLA-DP2: a molecular docking approach.Semantic proximity Read ↗

Clip binds to HLA class II using methionine-based, allele-dependent motifs as well as allele-independent supermotifs.Semantic proximity Read ↗

Modelling of HLA-DQ2 and its interaction with gluten peptides to explain molecular recognition in celiac disease.Semantic proximity Read ↗

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