Journal
CELL
Volume 134, Issue 1, Pages 124-134Publisher
CELL PRESS
DOI: 10.1016/j.cell.2008.05.051
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Funding
- Howard Hughes Medical Institute Funding Source: Medline
- NCI NIH HHS [R29 CA074305, R01 CA074305, R29 CA074305-04, R01 CA074305-07] Funding Source: Medline
- NIGMS NIH HHS [K99 GM080097] Funding Source: Medline
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The catalytic activity of the Src family of tyrosine kinases is suppressed byphosphorylation on a tyrosine residue located near the C terminus (Tyr 527 in c- Src), which is catalyzed by C-terminal Src Kinase (Csk). Given the promiscuity of most tyrosine kinases, it is remarkable that the C-terminal tails of the Src family kinases are the only known targets of Csk. We have determined the crystal structure of a complex between the kinase domains of Csk and c-Src at 2.9 angstrom resolution, revealing that interactions between these kinases position the C-terminal tail of c-Src at the edge of the active site of Csk. Csk cannot phosphorylate substrates that lack this docking mechanism because the conventional substrate binding site used by most tyrosine kinases to recognize substrates is destabilized in Csk by a deletion in the activation loop.
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