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Article

SH2-kinase linker mutations release Hck tyrosine kinase and transforming activities in Rat-2 fibroblasts.

The Journal of biological chemistry - 10 Sept 1999

Briggs S D, Smithgall T E

Abstract excerpt

Biochemical and structural studies of Src and related kinases demonstrate that two intramolecular interactions suppress kinase activity. These interactions involve binding of the SH2 domain to a phosphotyrosine residue in the C-terminal tail and association of the SH3 domain with a polyproline type II helix formed by amino acids linking the SH2 and kinase domains. Recent studies have shown that high affinity...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 10473622
DOI: 10.1074/jbc.274.37.26579

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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SH2-kinase linker mutations release Hck tyrosine kinase and transforming activities in Rat-2 fibroblasts.PMID 10473622Read ↗

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