Campaign Overview
- Campaigns
- 2
- Candidates
- 108
- Patches
- 6
- Top Generator Confidence
- 0.92
Target Identity
Structure Determination
- Title
- STAPHYLOCOCCAL ENTEROTOXIN B
- Method
- X-RAY DIFFRACTION
- Deposited
- November 26, 1997
- Released
- May 27, 1998
- Molecular Weight
- 28.3 kDa
- Polymer Entities
- 1
Primary Publication
Crystal structure of microbial superantigen staphylococcal enterotoxin B at 1.5 A resolution: implications for superantigen recognition by MHC class II molecules and T-cell receptors.
Function & Biology
Recommended Name
Enterotoxin type B
Gene Names
Molecular Function
Staphylococcal enterotoxin that activates the host immune system by binding as unprocessed molecules to major histocompatibility (MHC) complex class II and T-cell receptor (TCR) molecules. In turn, this ternary complex activates a large number of T-lymphocytes initiating a systemic release of pro-inflammatory cytokines (PubMed:2303780, PubMed:25015819). Also causes the intoxication staphylococcal food poisoning syndrome (By similarity)
Known Interactions
Protein-protein interactions curated by UniProt. Understanding native binding partners can inform competitive binder strategies and help validate target binding sites.
Related Articles
Staphylococcal Enterotoxin B: A Computational Binder Campaign on a Superantigen Target
A full AffiniBind campaign against staphylococcal enterotoxin B generated 33 candidate binders across three source tools, resolving one epitope from six identified patches and ranking candidates through a twelve-dimension developability assessment.
Computational Protein Engineering14 min read
Engineering De Novo Binders Against Staphylococcal Enterotoxin B with the AffiniBind Pipeline
A full AffiniBind campaign against Staphylococcal Enterotoxin B generated 83 candidate binders across three generator tools, resolved six binding patches, and ranked candidates by generator confidence with developability metrics including PRODIGY ΔG, 3D-SAP, and PROPKA pI.
Computational Protein Engineering10 min read