Possible conformation of major histocompatibility antigens: implication of amino acid sequence data.
Possible conformation of major histocompatibility antigens was proposed on the basis of homology between domains of major histocompatibility antigen polypeptide chains and domains of immunoglobulins, characterized by a beta-pleated structure. In the hypothetical three-dimensional structure, domains alpha 3 and alpha 2 interact along the chain similarly to the CH2 and CH3 domains of IgG. beta 2-Microglobulin together with domain alpha 2 forms a structure analogous to the CH3--CH3 or CH1--CL dimers in IgG. Domains alpha 2 ans alpha 1 interact in such a manner that the beta-pleated sheet of domain alpha 2 is directly joined to the beta-pleated sheet of domain alpha 1. Hypervariable regions in domains alpha 1 and alpha 2, which most likely take part in the formation of the alloantigen determinants, represent the loops joining the regions of the beta-pleated structure. Domains alpha 1 and alpha 2 may be packed in such a way that their hypervariable regions would become adjacent and would be located on their surface turned aside from the surface of the cell membrane.
D000595:Amino Acid Sequence; D002942:Circular Dichroism; D006680:HLA Antigens / Q000032:analysis*; D006801:Humans; D007141:Immunoglobulin Fc Fragments / Q000032:analysis; D007074:Immunoglobulin G / Q000032:analysis; D066298:In Vitro Techniques; D011487:Protein Conformation
D006680:HLA Antigens; D007141:Immunoglobulin Fc Fragments; D007074:Immunoglobulin G