1inq: Difference between revisions

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{{STRUCTURE_1inq|  PDB=1inq  |  SCENE=  }}  
{{STRUCTURE_1inq|  PDB=1inq  |  SCENE=  }}  


'''Structure of Minor Histocompatibility Antigen peptide, H13a, complexed to H2-Db'''
===Structure of Minor Histocompatibility Antigen peptide, H13a, complexed to H2-Db===




==Overview==
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The mouse H13 minor histocompatibility (H) Ag, originally detected as a barrier to allograft transplants, is remarkable in that rejection is a consequence of an extremely subtle interchange, P4(Val/Ile), in a nonamer H2-D(b)-bound peptide. Moreover, H13 peptides lack the canonical P5(Asn) central anchor residue normally considered important for forming a peptide/MHC complex. To understand how these noncanonical peptide pMHC complexes form physiologically active TCR ligands, crystal structures of allelic H13 pD(b) complexes and a P5(Asn) anchored pD(b) analog were solved to high resolution. The structures show that the basis of TCRs to distinguish self from nonself H13 peptides is their ability to distinguish a single solvent-exposed methyl group. In addition, the structures demonstrate that there is no need for H13 peptides to derive any stabilization from interactions within the central C pocket to generate fully functional pMHC complexes. These results provide a structural explanation for a classical non-MHC-encoded H Ag, and they call into question the requirement for contact between anchor residues and the major MHC binding pockets in vaccine design.
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{{ABSTRACT_PUBMED_11751972}}


==About this Structure==
==About this Structure==
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[[Category: Mhc complex]]
[[Category: Mhc complex]]
[[Category: Minor histocompatibility antigen]]
[[Category: Minor histocompatibility antigen]]
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