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

Zinc binding and dimerization of Streptococcus pyogenes pyrogenic exotoxin C are not essential for T-cell stimulation.

The Journal of biological chemistry - 14 Mar 2003

Swietnicki Wieslaw, Barnie Anne M, Dyas Beverly K, Ulrich Robert G

Abstract excerpt

Streptococcal pyrogenic enterotoxin C (Spe-C) is a superantigen virulence factor produced by Streptococcus pyogenes that activates T-cells polyclonally. The biologically active form of Spe-C is thought to be a homodimer containing an essential zinc coordination site on each subunit, consisting of the residues His(167), His(201), and Asp(203). Crystallographic data suggested that receptor specificity is dependent...

Read the complete abstract on PubMed

Topics

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

Share to Antigens
Share to Binding, Competitive

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cations

Share to Chromatography, Gel

Share to Chromatography, Liquid

Share to Streptococcus pyogenes

Share to Surface Plasmon Resonance

Source

Identifiers

PMID: 12473669
DOI: 10.1074/jbc.M206957200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Zinc binding and dimerization of Streptococcus pyogenes pyrogenic exotoxin C are not essential for T-cell stimulation.PMID 12473669Read ↗

Identification and Characterization of Novel Superantigens from <i>Streptococcus pyogenes </i>Semantic proximity Read ↗

Conservation and variation in superantigen structure and activity highlighted by the three-dimensional structures of two new superantigens from Streptococcus pyogenes.Semantic proximity Read ↗

Streptococcal superantigen, mitogenic factor, and pyrogenic exotoxin B expressed by Streptococcus pyogenes. Structure and function.Semantic proximity Read ↗

Structural features of a zinc binding site in the superantigen strepococcal pyrogenic exotoxin A (SpeA1): implications for MHC class II recognition.Semantic proximity Read ↗

The bacterial superantigen streptococcal mitogenic exotoxin Z is the major immunoactive agent of Streptococcus pyogenes.Semantic proximity Read ↗

Crystal structure of Streptococcus dysgalactiae-derived mitogen reveals a zinc-binding site and alterations in TcR binding.Semantic proximity Read ↗

Mutations affecting MHC class II binding of the superantigen streptococcal erythrogenic toxin A.Semantic proximity Read ↗

Analysis of the interaction between the bacterial superantigen streptococcal pyrogenic exotoxin A (SpeA) and the human T-cell receptor.Semantic proximity Read ↗

Analysis of the superantigenic activity of mutant and allelic forms of streptococcal pyrogenic exotoxin A.Semantic proximity Read ↗

HLA Class II Polymorphisms Determine Responses to Bacterial SuperantigensSemantic proximity Read ↗

Peripheral blood T cell responses to keratin peptides that share sequences with streptococcal M proteins are largely restricted to skin-homing CD8+ T cellsSemantic proximity Read ↗

Superantigenicity of streptococcal M protein.Semantic proximity Read ↗

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