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A Mouse MHC Class I Molecule (H-2Kb)/Peptide Complex
MHC class I molecules are expressed on the surfaces of most cells and are recognized by CD8-positive cytotoxic TC-cells, an essential step for initiating the elimination of virally infected cells by TC-cell-mediated lysis.  Below is an image of the molecular complex between a soluble fragment of murine H-2Kb and a 9-amino-acid nucleoprotein peptide of Sendai Virus (SEV-9).

1) of the extracellular domains of the H-2Kb (αβ2m) heterodimer
2) formed by a network of anti-parallel -strands and 2 α-helices, traced at one point here in the N-to-C direction, starting in α1 and ending in α2.
3) of SEV-9 peptide binding to the α1α2 membrane-distal domains of H-2Kb.  Note the positions of the 9 H2O molecules.
4) exposing the interior positions of 9 H2O molecules that effectively form the "glue" that stabilizes the peptide and MHC pocket interaction.
5) the α3 membrane-proximal domain immunoglobulin fold.
6) β2m subunit immunoglobulin fold.
Color coding:
  • α1, α2 , and α3 = a subunit domains of H-2Kb
  • β2m = β-2 microglobulin subunit
  • O2 atoms of H2O molecules (the H atoms are not visible)
  • SEV-9 = Sendai Virus nucleoprotein peptide (Phe-Ala-Pro-Gly-Asn-Tyr-Pro-Ala-Leu) bound to the α1,α2 antigen binding pocket of H-2Kb.

Overview of MHC class I three-dimensional structure.
Animation of dual peptide binding by one MHC class I molecule.
Overview of MHC class II three-dimensional structure.
Animation of MHC class II domain structure.
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© Duane W. Sears
August 29, 2009