Article
Autoinhibition of Bcr-Abl through its SH3 domain.
Molecular cell - 1 Jul 2003
Smith Kristen M, Yacobi Rinat, Van Etten Richard A
Abstract excerpt
Bcr-Abl is a dysregulated tyrosine kinase whose mechanism of activation is unclear. Here, we demonstrate that, like c-Abl, Bcr-Abl is negatively regulated through its SH3 domain. Kinase activity, transformation, and leukemogenesis by Bcr-Abl are greatly impaired by mutations of the Bcr coiled-coil domain that disrupt oligomerization, but restored by an SH3 point mutation that blocks ligand binding or a...
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