Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Single MHC mutation eliminates enthalpy associated with T cell receptor binding.

Journal of molecular biology - 19 Oct 2007

Miller Peter J, Pazy Yael, Conti Brian, Riddle David, Appella Ettore, Collins Edward J

Abstract excerpt

The keystone of the adaptive immune response is T cell receptor (TCR) recognition of peptide presented by major histocompatibility complex (pMHC) molecules. The crystal structure of AHIII TCR bound to MHC, HLA-A2, showed a large interface with an atypical binding orientation. MHC mutations in the...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Binding Sites
Share to Cells, Cultured
Share to HLA-A2 Antigen

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Major Histocompatibility Complex

Share to Models, Molecular

Share to Receptors, Antigen, T-Cell

Share to Surface Plasmon Resonance

Share to Thermodynamics

Source

Open in PubMed Open full text

Identifiers

PMID: 17825839
DOI: 10.1016/j.jmb.2007.07.028
PMCID: PMC2065754

Genes

CDR2

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-17825839-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Single MHC mutation eliminates enthalpy associated with T cell receptor binding.PMID 17825839Read ↗

Unraveling a hotspot for TCR recognition on HLA-A2: evidence against the existence of peptide-independent TCR binding determinants.Semantic proximity Read ↗

High-affinity T cell receptor differentiates cognate peptide-MHC and altered peptide ligands with distinct kinetics and thermodynamics.Semantic proximity Read ↗

The contribution of major histocompatibility complex contacts to the affinity and kinetics of T cell receptor binding.Semantic proximity Read ↗

The basis for limited specificity and MHC restriction in a T cell receptor interface.Semantic proximity Read ↗

Structural basis for the restoration of TCR recognition of an MHC allelic variant by peptide secondary anchor substitution.Semantic proximity Read ↗

MHC class I-peptide interactions and TCR recognition.Semantic proximity Read ↗

Mutations in MHC class II dimer of dimers contact residues: effects on antigen presentation.Semantic proximity Read ↗

CDR3 binding chemistry controls TCR V-domain rotational probability and germline CDR2 scanning of polymorphic MHCSemantic proximity Read ↗

T-cell receptor specificity maintained by altered thermodynamics.Semantic proximity Read ↗

The crystal structures of K(bm1) and K(bm8) reveal that subtle changes in the peptide environment impact thermostability and alloreactivity.Semantic proximity Read ↗

Interactions among polymorphic and conserved residues in MHC class II proteins affect MHC-peptide conformation and T cell recognition.Semantic proximity Read ↗

An Engineered Switch in T Cell Receptor Specificity Leads to an Unusual but Functional Binding Geometry.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.