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Article

Structural elements that regulate pp59c-fyn catalytic activity, transforming potential, and ability to associate with polyomavirus middle-T antigen.

Journal of virology - 1 Jan 1991

Cheng S H, Espino P C, Marshall J, Harvey R, Merrill J, Smith A E

Abstract excerpt

Except for its unique amino-terminal region (residues 1 through 83), which possibly dictates substrate recognition, pp59c-fyn bears a high degree of homology with other members of the src family of tyrosine kinases. Here we show that the carboxy terminus of pp59c-fyn is necessary for stable middle-T-antigen association, that pp59c-fyn is normally phosphorylated on both serine and tyrosine residues, and that...

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Identifiers

PMID: 1985196
DOI: 10.1128/JVI.65.1.170-179.1991
PMCID: PMC240502

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