The solution structure of a class II major histocompatibility complex superantigen binding domain

Academic Article

Abstract

  • We have used 600 MHz 1H NMR spectroscopy data to determine the solution structure of a 31-residue domain of a murine class II major histocompatibility (MHC) protein. This domain, I-A(β)b-(60-90), binds to the superantigen staphylococcal enterotoxin A. Distance geometry and dynamical simulated annealing calculations were performed using NOESY- and COSY-deduced constraints. I-A(β)b-(60-90), which is mostly α-helical, is more similar to the corresponding region of the class II MHC protein HLA-DR1 than to the class I MHC protein HLA-A2. Arg-72 and Arg-80 lie on the same side of the helix and face away from the antigenic peptide binding groove. His-81, implicated in both superantigen and peptide binding, is located midway between the surface defined by Arg-72/Arg-80 and residues that define the inside of the peptide binding groove, allowing for its participation in both types of binding.
  • Digital Object Identifier (doi)

    Author List

  • Jablonsky MJ; Subramaniam PS; Johnson HM; Russell JK; Krishna NR
  • Start Page

  • 660
  • End Page

  • 665
  • Volume

  • 234
  • Issue

  • 3