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

Johnsson, Kai¹  Johnsson, Nils¹  Weber, Klaus¹ 

[1] Max Planck Institute for Biophysical Chemistry, D-34 Göttingen, FRG

关键词: Calpactin;    Discontinuous epitope;    Lipocortin;    src kinase;    Tyrosine phosphate;   

DOI  :  10.1016/0014-5793(88)80314-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown