(Q27677334)

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The Energetic Basis Underpinning T-cell Receptor Recognition of a Super-bulged Peptide Bound to a Major Histocompatibility Complex Class I Molecule

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scholarly article

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The Energetic Basis Underpinning T-cell Receptor Recognition of a Super-bulged Peptide Bound to a Major Histocompatibility Complex Class I Molecule (English)

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6

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7

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James McCluskey

5

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Anthony W. Purcell

object named as

Anthony W Purcell

4

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Scott R Burrows

object named as

Scott R Burrows

3

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author name string

Yu Chih Liu

1

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Zhenjun Chen

2

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language of work or name

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publication date

6 April 2012

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Journal of Biological Chemistry

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287

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12267-76

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15

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Structural basis for the killing of human beta cells by CD8(+) T cells in type 1 diabetes

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A structural basis for varied αβ TCR usage against an immunodominant EBV antigen restricted to a HLA-B8 molecule

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A Role for Differential Variable Gene Pairing in Creating T Cell Receptors Specific for Unique Major Histocompatibility Ligands

1 reference

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T Cell Receptor Signaling Is Limited by Docking Geometry to Peptide-Major Histocompatibility Complex

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Structural basis for enabling T-cell receptor diversity within biased virus-specific CD8+ T-cell responses

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The impact of human leukocyte antigen (HLA) micropolymorphism on ligand specificity within the HLA-B*41 allotypic family

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Hard wiring of T cell receptor specificity for the major histocompatibility complex is underpinned by TCR adaptability

1 reference

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Constraints within major histocompatibility complex class I restricted peptides: Presentation and consequences for T-cell recognition

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PHENIX: a comprehensive Python-based system for macromolecular structure solution

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T cell allorecognition via molecular mimicry

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The shaping of T cell receptor recognition by self-tolerance

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Different Thermodynamic Binding Mechanisms and Peptide Fine Specificities Associated with a Panel of Structurally Similar High-Affinity T Cell Receptors † ‡

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The structural dynamics and energetics of an immunodominant T cell receptor are programmed by its Vbeta domain

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A T cell receptor flattens a bulged antigenic peptide presented by a major histocompatibility complex class I molecule

1 reference

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1 reference

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Two different, highly exposed, bulged structures for an unusually long peptide bound to rat MHC class I RT1-Aa

1 reference

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Features and development of Coot

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1 reference

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Phasercrystallographic software

1 reference

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20 March 2017

How TCRs bind MHCs, peptides, and coreceptors

1 reference

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IMGT, the international ImMunoGeneTics information system.

1 reference

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T-cell receptor bias and immunity

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Structural determinants of T-cell receptor bias in immunity

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TCR alpha genes direct MHC restriction in the potent human T cell response to a class I-bound viral epitope

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1 reference

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T cell receptor recognition of a 'super-bulged' major histocompatibility complex class I-bound peptide

1 reference

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High resolution structures of highly bulged viral epitopes bound to major histocompatibility complex class I. Implications for T-cell receptor engagement and T-cell immunodominance

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Toward a definition of self: proteomic evaluation of the class I peptide repertoire

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Antigen ligation triggers a conformational change within the constant domain of the alphabeta T cell receptor.

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Have we cut ourselves too short in mapping CTL epitopes?

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CTL recognition of a bulged viral peptide involves biased TCR selection

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The CDR3 regions of an immunodominant T cell receptor dictate the 'energetic landscape' of peptide-MHC recognition

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TCR binding to peptide-MHC stabilizes a flexible recognition interface

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based on heuristic

inferred from PubMed ID database lookup

Alanine scanning mutagenesis of an alphabeta T cell receptor: mapping the energy of antigen recognition

1 reference

https://pubmed.ncbi.nlm.nih.gov/22343629

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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