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

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 C...

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Veröffentlicht in:	FEBS letters 1986-03, Vol.198 (2), p.361-364
Hauptverfasser:	Johnsson, Nils, Vandekerckhove, Joel, Van Damme, Jozef, Weber, Klaus
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Animals Annexin A2 Annexins Binding Sites Biological and medical sciences Ca 2 Ca2 calcium Calcium - metabolism Calcium-Binding Proteins - metabolism Fundamental and applied biological sciences. Psychology Intestine Lipid Lipid Metabolism Membrane protein Membrane Proteins - analysis Microbiology p36 Peptides - metabolism Phosphorylation pigs Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains Retroviridae - enzymology S100 Proteins Swine Tryptophan - analysis Tyrosine - metabolism Tyrosine phosphate Virology
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Beschreibung
Zusammenfassung:	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.
ISSN:	0014-5793 1873-3468
DOI:	10.1016/0014-5793(86)80437-9