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

A mutational analysis of the binding of staphylococcal enterotoxins B and C3 to the T cell receptor beta chain and major histocompatibility complex class II.

The Journal of experimental medicine - 16 Mar 1998

Leder L, Llera A, Lavoie P M, Lebedeva M I, Li H, Sékaly R P, Bohach G A, Gahr P J, Schlievert P M, Karjalainen K, Mariuzza R A

Abstract excerpt

The three-dimensional structure of the complex between a T cell receptor (TCR) beta chain (mouse Vbeta8.2Jbeta2.1Cbeta1) and the superantigen (SAG) staphylococcal enterotoxin C3 (SEC3) has been recently determined to 3.5 resolution. To evaluate the actual contribution of individual SAG residues to stabilizing the beta-SEC3 complex, as well as to investigate the relationship between the affinity of SAGs for TCR...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Binding Sites

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Lymphocyte Activation

Share to Mice, Transgenic

Share to Molecular Sequence Data

Share to Mutation

Share to T-Lymphocytes

Source

Open in PubMed Open full text

Identifiers

PMID: 9500785
DOI: 10.1084/jem.187.6.823
PMCID: PMC2212189

Genes

SAG

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A mutational analysis of the binding of staphylococcal enterotoxins B and C3 to the T cell receptor beta chain and major histocompatibility complex class II.PMID 9500785Read ↗

Structure-function studies of T-cell receptor-superantigen interactions.Semantic proximity Read ↗

Subtype‐specific interactions of type C staphylococcal enterotoxins with the T‐cell receptorSemantic proximity Read ↗

Mutational analysis of the binding of staphylococcal enterotoxin D to the T cell receptor Vbeta chain and major histocompatibility complex class II.Semantic proximity Read ↗

High affinity T cell receptors from yeast display libraries block T cell activation by superantigens.Semantic proximity Read ↗

A mutation of F47 to A in staphylococcus enterotoxin A activates the T-cell receptor Vbeta repertoire in vivo.Semantic proximity Read ↗

Staphylococcus aureus isolates encode variant staphylococcal enterotoxin B proteins that are diverse in superantigenicity and lethality.Semantic proximity Read ↗

Predictions of T-cell receptor- and major histocompatibility complex-binding sites on staphylococcal enterotoxin C1.Semantic proximity Read ↗

The domain structure and functional relationships in the bacterial superantigen, SEB.Semantic proximity Read ↗

Structural basis for abrogated binding between staphylococcal enterotoxin A superantigen vaccine and MHC-IIalpha.Semantic proximity Read ↗

Molecular characterization of the putative T-cell receptor cavity of the superantigen staphylococcal enterotoxin B.Semantic proximity Read ↗

Molecular basis of TCR selectivity, cross-reactivity, and allelic discrimination by a bacterial superantigen: integrative functional and energetic mapping of the SpeC-Vbeta2.1 molecular interface.Semantic proximity Read ↗

Evaluation of a recombinant double mutant of staphylococcal enterotoxin B (SEB-H32Q/K173E) with enhanced antitumor activity effects and decreased pyrexia.Semantic proximity Read ↗

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