Four A6-TCR/peptide/HLA-A2 structures that generate very different T cell signals are nearly identical
about
Crystal structure of the human CD4 N-terminal two-domain fragment complexed to a class II MHC moleculeT cell receptor engagement triggers its CD3epsilon and CD3zeta subunits to adopt a compact, locked conformationA post-translational modification of nuclear proteins, N(G),N(G)-dimethyl-Arg, found in a natural HLA class I peptide ligandStructure of a complex of the human alpha/beta T cell receptor (TCR) HA1.7, influenza hemagglutinin peptide, and major histocompatibility complex class II molecule, HLA-DR4 (DRA*0101 and DRB1*0401): insight into TCR cross-restriction and alloreactivQuantitative challenges in understanding ligand discrimination by alphabeta T cellsThe multiple roles of the CD8 coreceptor in T cell biology: opportunities for the selective modulation of self-reactive cytotoxic T cellsSurface-anchored monomeric agonist pMHCs alone trigger TCR with high sensitivityStructure of a covalently stabilized complex of a human alphabeta T-cell receptor, influenza HA peptide and MHC class II molecule, HLA-DR1Class I major histocompatibility complex anchor substitutions alter the conformation of T cell receptor contactsT cell activity correlates with oligomeric peptide-major histocompatibility complex binding on T cell surfaceStructural Comparison of Allogeneic and Syngeneic T Cell Receptor–Peptide-Major Histocompatibility Complex ComplexesA T cell receptor flattens a bulged antigenic peptide presented by a major histocompatibility complex class I moleculeHow much can a T-cell antigen receptor adapt to structurally distinct antigenic peptides?Structures of MART-126/27–35 Peptide/HLA-A2 Complexes Reveal a Remarkable Disconnect between Antigen Structural Homology and T Cell RecognitionSingle MHC Mutation Eliminates Enthalpy Associated with T Cell Receptor BindingCitrullination-dependent differential presentation of a self-peptide by HLA-B27 subtypesGerm Line-governed Recognition of a Cancer Epitope by an Immunodominant Human T-cell ReceptorFluorine substitutions in an antigenic peptide selectively modulate T-cell receptor binding in a minimally perturbing mannerStructural Evaluation of Potent NKT Cell Agonists: Implications for Design of Novel Stimulatory LigandsT Cell Receptor Cross-reactivity Directed by Antigen-Dependent Tuning of Peptide-MHC Molecular FlexibilityRigid-body Ligand Recognition Drives Cytotoxic T-lymphocyte Antigen 4 (CTLA-4) Receptor TriggeringConformational Melding Permits a Conserved Binding Geometry in TCR Recognition of Foreign and Self Molecular MimicsLoss of T Cell Antigen Recognition Arising from Changes in Peptide and Major Histocompatibility Complex Protein Flexibility: IMPLICATIONS FOR VACCINE DESIGNDisparate Degrees of Hypervariable Loop Flexibility Control T-Cell Receptor Cross-Reactivity, Specificity, and Binding MechanismT Cell Receptor Signaling Is Limited by Docking Geometry to Peptide-Major Histocompatibility ComplexT Cell Receptors are Structures Capable of Initiating Signaling in the Absence of Large Conformational RearrangementsCrossreactivity of a human autoimmune TCR is dominated by a single TCR loopT-cell Receptor (TCR)-Peptide Specificity Overrides Affinity-enhancing TCR-Major Histocompatibility Complex InteractionsA molecular basis underpinning the T cell receptor heterogeneity of mucosal-associated invariant T cellsPeptide modulation of class I major histocompatibility complex protein molecular flexibility and the implications for immune recognition.Structural basis of affinity maturation and intramolecular cooperativity in a protein-protein interactionStructure of a TCR-Mimic Antibody with Target Predicts Pharmacogenetics.DynaDom: structure-based prediction of T cell receptor inter-domain and T cell receptor-peptide-MHC (class I) association angles.The quantum chemical causality of pMHC-TCR biological avidity: Peptide atomic coordination data and the electronic state of agonist N termini.The SCHOOL of nature: I. Transmembrane signaling.The effect of mutations on the alloreactive T cell receptor/peptide-MHC interface structure: a molecular dynamics study.How structural adaptability exists alongside HLA-A2 bias in the human αβ TCR repertoireStructure-based design of a T-cell receptor leads to nearly 100-fold improvement in binding affinity for pepMHC.Understanding TR binding to pMHC complexes: how does a TR scan many pMHC complexes yet preferentially bind to one.POPISK: T-cell reactivity prediction using support vector machines and string kernels.
P2860
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P2860
Four A6-TCR/peptide/HLA-A2 structures that generate very different T cell signals are nearly identical
description
1999 nî lūn-bûn
@nan
1999 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Four A6-TCR/peptide/HLA-A2 str ...... l signals are nearly identical
@ast
Four A6-TCR/peptide/HLA-A2 str ...... l signals are nearly identical
@en
Four A6-TCR/peptide/HLA-A2 str ...... l signals are nearly identical
@nl
type
label
Four A6-TCR/peptide/HLA-A2 str ...... l signals are nearly identical
@ast
Four A6-TCR/peptide/HLA-A2 str ...... l signals are nearly identical
@en
Four A6-TCR/peptide/HLA-A2 str ...... l signals are nearly identical
@nl
prefLabel
Four A6-TCR/peptide/HLA-A2 str ...... l signals are nearly identical
@ast
Four A6-TCR/peptide/HLA-A2 str ...... l signals are nearly identical
@en
Four A6-TCR/peptide/HLA-A2 str ...... l signals are nearly identical
@nl
P2093
P3181
P1433
P1476
Four A6-TCR/peptide/HLA-A2 str ...... l signals are nearly identical
@en
P2093
D N Garboczi
W E Biddison
P3181
P356
10.1016/S1074-7613(00)80080-1
P407
P577
1999-07-01T00:00:00Z