Binding sites for calcium, lipid and p11 on p36, the substrate of retroviral tyrosine‐specific protein kinases

FEBS Letters

Johnsson, Nils¹  Weber, Klaus¹  Van Damme, Jozef²  Vandekerckhove, Joel² 

[1] Max Planck Institute for Biophysical Chemistry, D-3400 Göttingen, FRG;Rijksuniversiteit Gent, Laboratory of Genetics, B-9000 Gent, Belgium

关键词: Ca2+;    (Intestine);    Lipid;    Membrane protein;    Tyrosine phosphate;   

DOI  :  10.1016/0014-5793(86)80437-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Biochemical and partial sequence data reveal the two-domain structure of p36. A loose structure of some 30 residues at the amino-terminus contains the phosphorylatable tyrosine and the binding site for the p11 regulatory chain. The following p33 domain retains the lipid-binding site as well as the Ca²⁺ site which influences the spectral properties of the single tryptophan and one tyrosine. The combined sequence data covering about 25% of the molecule identify p36 as a unique polypeptide.

【 授权许可】

Unknown