Microbiology and Immunology 3300B Lecture : Immunology Notes

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Mhc class ii molecules have an open conformation where longer peptides can fit. They are made of and chains, made of two genes, and each gene has two alleles, and there are many different alleles possible. The 2 and 2 domains are transmembrane domains. The peptide-binding cleft is made of the 1 and 1 domains, but they are not joined by a covalent bond. The peptide-binding groove is open at both ends. Peptide binding to mhc class ii molecules is stabilized by numerous contact points. They bind all along the length of the binding groove, not just at the ends like class i. There are hydrophobic or hydrophilic interactions and hydrogen bonds between the peptide and the mhc molecule. The average peptide binding to class ii molecules is 13-17 amino acid residues (length is not constrained). Anchor residues or contact points lie at various distances from the ends of the peptide. The location is different for every class ii molecule.

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