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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 Ca2+/lipid-binding proteins.

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Johnsson,  N.
Department of Biochemistry and Cell Biology, MPI for biophysical chemistry, Max Planck Society;

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Weber,  K.
Department of Biochemistry and Cell Biology, MPI for biophysical chemistry, Max Planck Society;

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Johnsson, N., Johnsson, K., & Weber, K. (1988). 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 Ca2+/lipid-binding proteins. FEBS Letters, 236(1), 201-204. doi:10.1016/0014-5793(88)80314-4.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002D-4BB2-A
Abstract
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 Ca2+/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 Ca2+ requirement of the modified p36 in phospholipid binding.