HLA-DM targets the hydrogen bond between the histidine at position beta81 and peptide to dissociate HLA-DR-peptide complexes. - Wikidata - wikimedia - TriplyDB

HLA-DM targets the hydrogen bond between the histidine at position beta81 and peptide to dissociate HLA-DR-peptide complexes.

HLA-DM targets the hydrogen bond between the histidine at position beta81 and peptide to dissociate HLA-DR-peptide complexes.

http://www.wikidata.org/entity/Q34483195

about

A step-by-step overview of the dynamic process of epitope selection by major histocompatibility complex class II for presentation to helper T cells MHC Class II Auto-Antigen Presentation is Unconventional Staphylococcal enterotoxin A induces small clusters of HLA-DR1 on B cells The Peptide-Receptive Transition State of MHC Class I Molecules: Insight from Structure and Molecular Dynamics HLA-DO acts as a substrate mimic to inhibit HLA-DM by a competitive mechanism Conformational lability in the class II MHC 310 helix and adjacent extended strand dictate HLA-DM susceptibility and peptide exchange Disruption of Hydrogen Bonds between Major Histocompatibility Complex Class II and the Peptide N-Terminus Is Not Sufficient to Form a Human Leukocyte Antigen-DM Receptive State of Major Histocompatibility Complex Class II Susceptibility to HLA-DM Protein Is Determined by a Dynamic Conformation of Major Histocompatibility Complex Class II Molecule Bound with Peptide Exogenous antigens bind MHC class II first, and are processed by cathepsins later HLA-DM captures partially empty HLA-DR molecules for catalyzed removal of peptide Anchor side chains of short peptide fragments trigger ligand-exchange of class II MHC molecules Model for the peptide-free conformation of class II MHC proteins.Identification of the transcriptional response of human intestinal mucosa to Lactobacillus plantarum WCFS1 in vivo.HLA-DM mediates epitope selection by a "compare-exchange" mechanism when a potential peptide pool is available.An unstable Th epitope of P. falciparum fosters central memory T cells and anti-CS antibody responses.Characterization of structural features controlling the receptiveness of empty class II MHC molecules.Cutting edge: HLA-DM functions through a mechanism that does not require specific conserved hydrogen bonds in class II MHC-peptide complexes.Complexes of two cohorts of CLIP peptides and HLA-DQ2 of the autoimmune DR3-DQ2 haplotype are poor substrates for HLA-DM For many but not for all: how the conformational flexibility of the peptide/MHCII complex shapes epitope selection Divergent paths for the selection of immunodominant epitopes from distinct antigenic sources.A reductionist cell-free major histocompatibility complex class II antigen processing system identifies immunodominant epitopes.The convergent roles of tapasin and HLA-DM in antigen presentation.HLA-DO as the optimizer of epitope selection for MHC class II antigen presentation.Evaluating the Role of HLA-DM in MHC Class II-Peptide Association Reactions.The Thermodynamic Mechanism of Peptide-MHC Class II Complex Formation Is a Determinant of Susceptibility to HLA-DM.Empty class II major histocompatibility complex created by peptide photolysis establishes the role of DM in peptide association.Immunodominance in CD4 T-cell responses: implications for immune responses to influenza virus and for vaccine design.Thermodynamics of Peptide-MHC Class II Interactions: Not all Complexes are Created Equal.The control of the specificity of CD4 T cell responses: thresholds, breakpoints, and ceilings HLA-DM mediates peptide exchange by interacting transiently and repeatedly with HLA-DR1.Enhanced silencing and stabilization of siRNA polyplexes by histidine-mediated hydrogen bonds.Conformational heterogeneity of MHC class II induced upon binding to different peptides is a key regulator in antigen presentation and epitope selection.Conformational variation in structures of classical and non-classical MHCII proteins and functional implications.HLA-DM: arbiter conformationis.Re-Directing CD4(+) T Cell Responses with the Flanking Residues of MHC Class II-Bound Peptides: The Core is Not Enough.Structural Characteristics of HLA-DQ that May Impact DM Editing and Susceptibility to Type-1 Diabetes.HLA-DM Focuses on Conformational Flexibility Around P1 Pocket to Catalyze Peptide Exchange.Measurement of Peptide Binding to MHC Class II Molecules by Fluorescence Polarization.Structural Insights Into HLA-DM Mediated MHC II Peptide Exchange.Determinants of immunodominance for CD4 T cells.

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HLA-DM targets the hydrogen bond between the histidine at position beta81 and peptide to dissociate HLA-DR-peptide complexes.

http://www.wikidata.org/entity/Q34483195

description

2006 nî lūn-bûn

@nan

2006 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2006 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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2006年の論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年论文

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name

HLA-DM targets the hydrogen bo ...... iate HLA-DR-peptide complexes.

@ast

HLA-DM targets the hydrogen bo ...... iate HLA-DR-peptide complexes.

@en

HLA-DM targets the hydrogen bo ...... iate HLA-DR-peptide complexes.

@nl

type

label

HLA-DM targets the hydrogen bo ...... iate HLA-DR-peptide complexes.

@ast

HLA-DM targets the hydrogen bo ...... iate HLA-DR-peptide complexes.

@en

HLA-DM targets the hydrogen bo ...... iate HLA-DR-peptide complexes.

@nl

prefLabel

HLA-DM targets the hydrogen bo ...... iate HLA-DR-peptide complexes.

@ast

HLA-DM targets the hydrogen bo ...... iate HLA-DR-peptide complexes.

@en

HLA-DM targets the hydrogen bo ...... iate HLA-DR-peptide complexes.

@nl

P1433

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P1433

Nature Immunology

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HLA-DM targets the hydrogen bo ...... ciate HLA-DR-peptide complexes

@en

P2093

AeRyon Kim

http://www.w3.org/2001/XMLSchema#string

Chih-Ling Chou

http://www.w3.org/2001/XMLSchema#string

Isamu Z Hartman

http://www.w3.org/2001/XMLSchema#string

Kedar Narayan

http://www.w3.org/2001/XMLSchema#string

Sarat Dalai

http://www.w3.org/2001/XMLSchema#string

P2860

HLA-DM induces CLIP dissociation from MHC class II alpha beta dimers and facilitates peptide loading

Mutations changing the kinetics of class II MHC peptide exchange

Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide

Structures of an MHC class II molecule with covalently bound single peptides

The class II MHC protein HLA-DR1 in complex with an endogenous peptide: implications for the structural basis of the specificity of peptide binding

Crystal structure of I-Ak in complex with a dominant epitope of lysozyme

Interaction of HLA-DR with an acidic face of HLA-DM disrupts sequence-dependent interactions with peptides

H2-M mutant mice are defective in the peptide loading of class II molecules, antigen presentation, and T cell repertoire selection

Mice lacking H2-M complexes, enigmatic elements of the MHC class II peptide-loading pathway

Antigen presentation and T cell development in H2-M-deficient mice

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92-100

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scholarly article

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10.1038/NI1414

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1

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8

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Scheherazade Sadegh-Nasseri

Stanislav Khoruzhenko

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2006-12-03T00:00:00Z

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232796071

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17143275

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3019572

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