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A discontinuous epitope on p36, the major substrate of src tyrosine‐protein‐kinase, brings the phosphorylation site into the neighbourhood of a consensus sequence for Ca 2+ /lipid‐binding proteins
Author(s) -
Johnsson Nils,
Johnsson Kai,
Weber Klaus
Publication year - 1988
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(88)80314-4
Subject(s) - phosphorylation , epitope , binding site , tyrosine , biochemistry , chemistry , protein tyrosine phosphatase , phosphotyrosine binding domain , peptide , plasma protein binding , consensus sequence , biology , peptide sequence , microbiology and biotechnology , antibody , sh2 domain , gene , immunology
Previous models of p36 based on proteolytic fragments describe the tail and core as two noninteracting domains. However, the monoclonal antibody H28 recognizes a discontinuous epitope, which covers the peptide segments around Ser 25 in the tail and around Glu 65 in the core of porcine p36. Thus, the phosphorylatable Tyr 23 is much closer to the first consensus sequence (residues 46–62) of Ca 2+ /lipid‐binding proteins than previously thought. This apposition is in line with biochemical experiments indicating an influence of core ligands on tyrosine phosphorylation and an enhanced Ca 2+ requirement of the modified p36 in phospholipid binding.