ArticlePloS one2020
Sequence-structure-function relationships in class I MHC: A local frustration perspective.
Article in PloS one, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 30 citations in OpenAlex.
- HLA micropolymorphisms confine neoantigen conformational adaptability and guide T cell receptor selectivity.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- HLA polymorphisms shape divergent outcomes of Toxoplasma and Plasmodium infection in Eastern Indian HbE/β-thalassemia cohort.Communications biology · 2026Article
- Article
- Differences in F pocket impact on HLA I genetic associations with autoimmune diabetes.Frontiers in immunology · 2024Article
- Molecular Characteristics, Functional Definitions, and Regulatory Mechanisms for Cross-Presentation Mediated by the Major Histocompatibility Complex: A Comprehensive Review.International journal of molecular sciences · 2023Review
- Conformational plasticity of RAS Q61 family of neoepitopes results in distinct features for targeted recognition.Nature communications · 2023Article
- Unsupervised and supervised AI on molecular dynamics simulations reveals complex characteristics of HLA-A2-peptide immunogenicity.Briefings in bioinformatics · 2023Article
- The Prognostic Significance of Selected HLA Alleles on Prostate Cancer Outcome.International journal of molecular sciences · 2023Article
- Brain Hydrophobic Peptides Antagonists of Neurotoxic Amyloid β Peptide Monomers/Oligomers-Protein Interactions.International journal of molecular sciences · 2023Review
- The 1926 novel, "One, no one, one hundred thousand", metaphorizes the potential danger when the immune system is exposed to a repetitive antigen stimulation.Frontiers in immunology · 2023Article
- Decoupling peptide binding from T cell receptor recognition with engineered chimeric MHC-I molecules.Frontiers in immunology · 2023Article
- Identification of novel interferon responsive protein partners of human leukocyte antigen A (HLA-A) using cross-linking mass spectrometry (CLMS) approach.Scientific reports · 2022Article
- PANDORA: A Fast, Anchor-Restrained Modelling Protocol for Peptide: MHC Complexes.Frontiers in immunology · 2022Article
- The pockets guide to HLA class I molecules.Biochemical Society transactions · 2021Review
- Dynamics of MHC-I molecules in the antigen processing and presentation pathway.Current opinion in immunology · 2021Review
- HLA-A29 and Birdshot Uveitis: Further Down the Rabbit Hole.Frontiers in immunology · 2020Review
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Class I Major Histocompatibility Complex (MHC) binds short antigenic peptides with the help of Peptide Loading Complex (PLC), and presents them to T-cell Receptors (TCRs) of cytotoxic T-cells and Killer-cell Immunglobulin-like Receptors (KIRs) of Natural Killer (NK) cells. With more than 10000 alleles, human MHC (Human Leukocyte Antigen, HLA) is the most polymorphic protein in humans. This allelic diversity provides a wide coverage of peptide sequence space, yet does not affect the three-dimensional structure of the complex. Moreover, TCRs mostly interact with HLA in a common diagonal binding mode, and KIR-HLA interaction is allele-dependent. With the aim of establishing a framework for understanding the relationships between polymorphism (sequence), structure (conserved fold) and function (protein interactions) of the human MHC, we performed here a local frustration analysis on pMHC homology models covering 1436 HLA I alleles. An analysis of local frustration profiles indicated that (1) variations in MHC fold are unlikely due to minimally-frustrated and relatively conserved residues within the HLA peptide-binding groove, (2) high frustration patches on HLA helices are either involved in or near interaction sites of MHC with the TCR, KIR, or tapasin of the PLC, and (3) peptide ligands mainly stabilize the F-pocket of HLA binding groove.
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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.