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Kellenberger, C ; Porciero, S ; Roussel, A

Expression, refolding, crystallization and preliminary crystallographic study of MHC H-2K(k) complexed with octapeptides and nonapeptides

Acta Crystallographica Section D-Biological Crystallography 60 1278-1280 Part 7

par Administrateur - publié le

Abstract :

Major histocompatibility complex (MHC) molecules are heterodimeric cell-surface receptors that play a crucial role in the cellular immune response by presenting epitope peptides to T-cell antigen receptors (TCR). Although the structural basis of the peptide - MHC binding mechanism is becoming better understood, it is still difficult to predict a binding mode for an MHC of unknown structure. Therefore, as the first stage of a TCR - MHC interaction study, the crystal structures of the mouse H-2K(k) molecule in complex with both an octapeptide from Influenza A virus and a nonapeptide from simian virus SV40 were solved.