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Binding sites for calcium, lipid and p11 on p36, the substrate of retroviral tyrosine‐specific protein kinases
Author(s) -
Johnsson Nils,
Vandekerckhove Joel,
Van Damme Jozef,
Weber Klaus
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)80437-9
Subject(s) - tyrosine , binding site , sequence (biology) , chemistry , tyrosine kinase , biochemistry , protein secondary structure , tryptophan , peptide sequence , amino acid , signal transduction , gene
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 Ca 2+ 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.