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

doi:10.1128/JVI.65.1.170-179.1991

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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...

Topics

Amino Acid Sequence
Animals
Antigens, Polyomavirus Transforming
Base Sequence
Cell Line
Chimera
Genetic Variation
Humans
Molecular Sequence Data
Mutagenesis, Site-Directed
Oligonucleotide Probes

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Peptide Mapping

Phosphopeptides

Phosphorylation

Plasmids

Protein Binding

Protein-Tyrosine Kinases

Proto-Oncogene Mas

Source

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Identifiers

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

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1985196-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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