1rk0: Difference between revisions

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[[Image:1rk0.jpg|left|200px]]
{{Seed}}
[[Image:1rk0.png|left|200px]]


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{{STRUCTURE_1rk0|  PDB=1rk0  |  SCENE=  }}  
{{STRUCTURE_1rk0|  PDB=1rk0  |  SCENE=  }}  


'''Mhc Class I H-2Kb Heavy Chain Complexed With beta-2 Microglobulin and Herpes Simplex Virus Glycoprotein B peptide'''
===Mhc Class I H-2Kb Heavy Chain Complexed With beta-2 Microglobulin and Herpes Simplex Virus Glycoprotein B peptide===




==Overview==
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Major histocompatibility complex (MHC) class I variants H-2K(b) and H-2K(bm8) differ primarily in the B pocket of the peptide-binding groove, which serves to sequester the P2 secondary anchor residue. This polymorphism determines resistance to lethal herpes simplex virus (HSV-1) infection by modulating T cell responses to the immunodominant glycoprotein B(498-505) epitope, HSV8. We studied the molecular basis of these effects and confirmed that T cell receptors raised against K(b)-HSV8 cannot recognize H-2K(bm8)-HSV8. However, substitution of Ser(P2) to Glu(P2) (peptide H2E) reversed T cell receptor (TCR) recognition; H-2K(bm8)-H2E was recognized whereas H-2K(b)-H2E was not. Insight into the structural basis of this discrimination was obtained by determining the crystal structures of all four MHC class I molecules in complex with bound peptide (pMHCs). Surprisingly, we find no concerted pMHC surface differences that can explain the differential TCR recognition. However, a correlation is apparent between the recognition data and the underlying peptide-binding groove chemistry of the B pocket, revealing that secondary anchor residues can profoundly affect TCR engagement through mechanisms distinct from the alteration of the resting state conformation of the pMHC surface.
The line below this paragraph, {{ABSTRACT_PUBMED_15557346}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_15557346}}


==About this Structure==
==About this Structure==
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[[Category: Tcr]]
[[Category: Tcr]]
[[Category: Virus]]
[[Category: Virus]]
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