ArticleImmunogenetics2013
Dynamics of free versus complexed β2-microglobulin and the evolution of interfaces in MHC class I molecules.
Article in Immunogenetics, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Conformational flexibility of a free and TCR-bound pMHC-I protein investigated by long-term molecular dynamics simulations.BMC immunology · 2022Article
- The Structure of a Peptide-Loaded Shark MHC Class I Molecule Reveals Features of the Binding between βJournal of immunology (Baltimore, Md. : 1950) · 2021Article
- Dynamics of MHC-I molecules in the antigen processing and presentation pathway.Current opinion in immunology · 2021Review
- Dynamically Driven Allostery in MHC Proteins: Peptide-Dependent Tuning of Class I MHC Global Flexibility.Frontiers in immunology · 2019Article
- Peptide exchange on MHC-I by TAPBPR is driven by a negative allostery release cycle.Nature chemical biology · 2018Article
- The Role of Molecular Flexibility in Antigen Presentation and T Cell Receptor-Mediated Signaling.Frontiers in immunology · 2018Review
- Major Histocompatibility Complex (MHC) Class I and MHC Class II Proteins: Conformational Plasticity in Antigen Presentation.Frontiers in immunology · 2017Review
- The Implication and Significance of Beta 2 Microglobulin: A Conservative Multifunctional Regulator.Chinese medical journal · 2016Review
- A Novel MHC-I Surface Targeted for Binding by the MCMV m06 Immunoevasin Revealed by Solution NMR.The Journal of biological chemistry · 2015Article
- The MHC class I genes of zebrafish.Developmental and comparative immunology · 2014Review
- A mechanistic basis for the co-evolution of chicken tapasin and major histocompatibility complex class I (MHC I) proteins.The Journal of biological chemistry · 2013Article
- NMR spectroscopy reveals unexpected structural variation at the protein-protein interface in MHC class I molecules.Journal of biomolecular NMR · 2013Article
- Extranodal induction of therapeutic immunity in the tumor microenvironment after intratumoral delivery of Tbet gene-modified dendritic cells.Cancer gene therapy · 2013Article
- Next generation sequencing analysis of human platelet PolyA+ mRNAs and rRNA-depleted total RNA.PloS one · 2013Article
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In major histocompatibility complex (MHC) class I molecules, monomorphic β(2)-microglobulin (β(2)m) is non-covalently bound to a heavy chain (HC) exhibiting a variable degree of polymorphism. β(2)M can stabilize a wide variety of complexes ranging from classical peptide binding to nonclassical lipid presenting MHC class I molecules as well as to MHC class I-like molecules that do not bind small ligands. Here we aim to assess the dynamics of individual regions in free as well as complexed β(2)m and to understand the evolution of the interfaces between β(2)m and different HC. Using human β(2)m and the HLA-B*27:09 complex as a model system, a comparison of free and HC-bound β(2)m by nuclear magnetic resonance spectroscopy was initially carried out. Although some regions retain their flexibility also after complex formation, these studies reveal that most parts of β(2)m gain rigidity upon binding to the HC. Sequence analyses demonstrate that some of the residues exhibiting flexibility participate in evolutionarily conserved β(2)m-HC contacts which are detectable in diverse vertebrate species or characterize a particular group of MHC class I complexes such as peptide- or lipid-binding molecules. Therefore, the spectroscopic experiments and the interface analyses demonstrate that β(2)m fulfills its role of interacting with diverse MHC class I HC as well as effector cell receptors not only by engaging in conserved intermolecular contacts but also by falling back upon key interface residues that exhibit a high degree of flexibility.
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