11Apr2003
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Our structural and functional studies
performed together with John Kuriyan's
group (UC Berkeley) reveal the mechanism of c-Abl autoregulation
by a novel myristoyl/phosphotyrosine switch.
We have recently published the structure of autoregulated c-Abl as well
as the complementary functional insights in Cell.
Click
here for abstracts, figures and PDB coordinates.
Click here for link to
Cell.
The
SH2 domain-phosphorylated tail interaction in Src family kinases is functionally
replaced in c-Abl by an intramolecular engagement of the N-terminal myristoyl
modification with the kinase domain.
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| We study Src and Abl,
both ubiquitous tyrosine kinases in higher organisms,
that participate in a variety of cellular functions
and have oncogenic (deregulated) counterparts.
Tyrosine phosphorylation
is particular because it is associated with key
decisions regarding the response of a cell to outside stimuli, like
cell growth after challenge by a growth factor.
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Investigating the regulation of a chosen
few prototypical tyrosine kinases may serve as key to the understanding
of more complex tyrosine phosphorylation phenomena.
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We analyse structure-function relationships in Src and Abl,
using conventional molecular biological techniques
and, in collaboration,
protein crystallography.
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