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[[Image:MHC I Structure.jpg|thumb|right|175px| Structure of MHC I molecule - Copyright Prof Dirk Werling DrMedVet PhD MRCVS]]

[[Image:MHC I Structure.jpg|thumb|right|175px| Structure of MHC I molecule - Copyright Prof Dirk Werling DrMedVet PhD MRCVS]]

The MHC class I domains are structurally and genetically related to immunoglobulin and TcR domains; the outer domains (&alpha1; and &alpha2;) are like the variable domains and the &alpha3; domain and &beta2m; are like the constant domains.

The MHC class I domains are structurally and genetically related to immunoglobulin and TcR domains; the outer domains (α1 and α2) are like the variable domains and the α3 domain and β2m are like the constant domains.

MHC class I molecules are folded to form specific 3-dimensional structures. The α1 and α2 domains are folded to produce an antigen-binding groove which can bind molecules of a limited size only (8-10 amino acids). This limits the size of epitope seen by the T-cell receptors.

MHC class I molecules are folded to form specific 3-dimensional structures. The α1 and α2 domains are folded to produce an antigen-binding groove which can bind molecules of a limited size only (8-10 amino acids). This limits the size of epitope seen by the T-cell receptors.