Tertiary structures for the extracellular domains of the epithelial polyimmunoglobulin receptor (secretory component) derived by primary structure comparisons with immunoglobulins.
The amino acid sequences of the rabbit receptor and human secretory component (SC) domains have been compared with those of immunoglobin (Ig) domains. Accessible and inaccessible sites of tryptic cleavage in bovine SC have been located by sequence homology. Computerized secondary structure prediction and three dimensional model building have been carried out. The resulting tertiary structures are extremely Ig-like consisting of two superposed beta-pleated sheets. All carbohydrate sites lie at external positions as do tryptic cleavage sites. Potential sites for tryptic hydrolysis that are not cleaved lie at buried or partially buried positions. 6. Inter-beta-sheet contact between domains appears to be highly unlikely so that the quaternary structure is largely determined by longitudinal contacts.
D000595:Amino Acid Sequence; D000818:Animals; D004848:Epithelium / Q000276:immunology; D006801:Humans; D007128:Immunoglobulin Fragments; D007136:Immunoglobulins; D046911:Macromolecular Substances; D011487:Protein Conformation; D011817:Rabbits; D011971:Receptors, Immunologic; D012635:Secretory Component; D013045:Species Specificity
D007128:Immunoglobulin Fragments; D007136:Immunoglobulins; D046911:Macromolecular Substances; D011971:Receptors, Immunologic; D012635:Secretory Component