Crystal structure of Hck in complex with a Src family-selective tyrosine kinase inhibitor (Q27618507)

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F Sicheri

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A Gazit

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A Levitzki

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J Kuriyan

Characterization of pp60c-src tyrosine kinase activities using a continuous assay: autoactivation of the enzyme is an intermolecular autophosphorylation process

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language of work or name

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May 1999

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published in

Molecular Cell

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volume

3

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page(s)

639-48

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issue

5

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cites work

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The role of the linker between the SH2 domain and catalytic domain in the regulation and function of Src.

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Activation and suppression of pp60c-src transforming ability by mutation of its primary sites of tyrosine phosphorylation

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Regulation by the autophosphorylation site in overexpressed pp60c-src

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Intramolecular regulatory interactions in the Src family kinase Hck probed by mutagenesis of a conserved tryptophan residue.

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Activation of the Src-family tyrosine kinase Hck by SH3 domain displacement

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Tyrosine phosphorylation regulates the biochemical and biological properties of pp60c-src

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Crystal structure of the Src family tyrosine kinase Hck

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Phosphorylation of tyrosine-416 is not required for the transforming properties and kinase activity of pp60v-src.

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SH2 domains recognize specific phosphopeptide sequences

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