The 3D Structure of Some Diarrheal Causing Bacterial Toxins

Abstract

The urgency to know the 3D structure of SEB is intensifying since there is a widespread effort currently to understand the mechanisms of its biological actions and of those of related staphylococcal enterotoxins (SEs), especially its toxicity and its extraordinary immunogenic activity, i.e., its superantigenicity. With respect to its role as a superantigen, certain amino acid residues in SEB have been demonstrated to be essential for interaction with the V beta T cell receptor while others have been shown to be crucial for binding with the MCH-II molecule, but the spatial relationships of these important functional residues remain unknown. The information will be evident in the 3D structure. The residues which target the V beta receptor are thought to be located close to each other on the protein surface although they occur in different parts of the amino acid sequence. The same investigators find that the MHC binding regions of SEB lie in the interior of the molecule. The protein accordingly is believed to undergo a change its conformation before it is able to bind to the MHC-II molecule.

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Document Details

Document Type
Technical Report
Publication Date
Jul 01, 1991
Accession Number
ADA242202

Entities

People

  • Martin Sax

Organizations

  • Veterans Administration Medical Center

Tags

Communities of Interest

  • Biomedical

DTIC Thesaurus Topics

  • Amino Acids
  • Bacterial Toxins
  • Biological Toxins
  • Cells
  • Classification
  • Diffraction
  • Electron Density
  • Electrons
  • Laboratory Animals
  • Lymphocytes
  • Materials
  • Molecular Structure
  • Molecules
  • Security
  • Three Dimensional
  • X Rays
  • X-Ray Diffraction

Readers

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