ReviewImmunological reviews2012
Conformational variation in structures of classical and non-classical MHCII proteins and functional implications.
Review in Immunological reviews, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
49 citing papers in PubMed, 76 citations in OpenAlex.
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- Potential contribution of gut microbiota in the development of autoantibodies in T1D children carrying HLA-DRB1/DQB1 risk alleles: an experimental and in silico analysis.Immunogenetics · 2024Article
- Determination of HLA class II risk alleles and prediction of self/non-self-epitopes contributing Hashimoto's thyroiditis in a group of Iranian patients.Immunogenetics · 2024Article
- Loading dynamics of one SARS-CoV-2-derived peptide into MHC-II revealed by kinetic models.Biophysical journal · 2023Article
- Identification of key immune-related genes in dilated cardiomyopathy using bioinformatics analysis.Scientific reports · 2023Article
- A class-mismatched TCR bypasses MHC restriction via an unorthodox but fully functional binding geometry.Nature communications · 2022Article
- Association of HLA-DQ Heterodimer Residues -18β and β57 With Progression From Islet Autoimmunity to Diabetes in the Diabetes Prevention Trial-Type 1.Diabetes care · 2022Article
- Peptide-dependent tuning of major histocompatibility complex motional properties and the consequences for cellular immunity.Current opinion in immunology · 2022Review
- Nine residues in HLA-DQ molecules determine with susceptibility and resistance to type 1 diabetes among young children in Sweden.Scientific reports · 2021Article
- Integrative Analysis of HTNV Glycoprotein Derived MHC II Epitopes byFrontiers in cellular and infection microbiology · 2021Article
- Structural Comparison Between MHC Classes I and II; in Evolution, a Class-II-Like Molecule Probably Came First.Frontiers in immunology · 2021Article
- A Simplified Amino Acidic Alphabet to Unveil the T-Cells Receptors Antigens: A Computational Perspective.Frontiers in chemistry · 2021Article
- Cartilaginous fish class II genes reveal unprecedented old allelic lineages and confirm the late evolutionary emergence of DM.Molecular immunology · 2020Article
- Human Hepatitis B Viral Infection Outcomes Are Linked to Naturally Occurring Variants ofJournal of immunology (Baltimore, Md. : 1950) · 2020Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Recent structural characterizations of classical and non-classical major histocompatibility complex class II (MHCII) proteins have provided a view into the dynamic nature of the MHCII-peptide binding groove and the role that structural changes play in peptide loading processes. Although there have been numerous reports of crystal structures for MHCII-peptide complexes, a detailed analysis comparing all the structures has not been reported, and subtle conformational variations present in these structures may not have been fully appreciated. We compared the 91 MHCII crystal structures reported in the PDB to date, including an HLA-DR mutant particularly susceptible to DM-mediated peptide exchange, and reviewed experimental and computational studies of the effect of peptide binding on MHCII structure. These studies provide evidence for conformational lability in and around the α-subunit 3-10 helix at residues α48-51, a region known to be critical for HLA-DM-mediated peptide exchange. A biophysical study of MHC-peptide hydrogen bond strengths and a recent structure of the non-classical MHCII protein HLA-DO reveal changes in the same region. Conformational variability was observed also in the vicinity of a kink in the β-subunit helical region near residue β66 and in the orientation and loop conformation in the β2 Ig domain. Here, we provide an overview of the regions within classical and non-classical MHCII proteins that display conformational changes and the potential role that these changes may have in the peptide loading/exchange process.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.