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Sequence analysis of bovine retinal S‐antigen
Author(s) -
Wistow Graeme J.,
Katial Albine,
Craft Cheryl,
Shinohara Toshimichi
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80207-1
Subject(s) - transducin , epitope , biology , antigen , microbiology and biotechnology , rhodopsin , complementary dna , monoclonal antibody , peptide sequence , biochemistry , antibody , retinal , genetics , gene
S‐Antigen is a major soluble protein of the retina and pineal. It is capable of inducing experimental autoimmune uveitis (EAU) in laboratory animals and also seems to play an important role in the visual cycle. The results of partial cDNA sequence analysis reveal interesting homologies with a‐transducin, a GTP‐binding protein of retina and other purine nucleotide‐binding proteins. In particular S‐antigen shows over 50% identity to the proposed pertussis toxin ADP‐ribosylation site of α‐transducin. It also contains the Gly‐X‐X‐X‐X‐Gly‐Lys pattern common to phosphoryl binding sites. A possible relationship between S‐antigen and purine nucleotide‐binding proteins is discussed. There is also evidence for a repetitious β‐structure in the C‐terminal half of S‐antigen, with a monoclonal antibody epitope in a helical region at the C‐terminus.