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PDBsum entry 2jfm
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References listed in PDB file
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Key reference
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Title
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Activation segment dimerization: a mechanism for kinase autophosphorylation of non-Consensus sites.
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Authors
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A.C.Pike,
P.Rellos,
F.H.Niesen,
A.Turnbull,
A.W.Oliver,
S.A.Parker,
B.E.Turk,
L.H.Pearl,
S.Knapp.
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Ref.
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Embo J, 2008,
27,
704-714.
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PubMed id
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Abstract
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Protein kinase autophosphorylation of activation segment residues is a common
regulatory mechanism in phosphorylation-dependent signalling cascades. However,
the molecular mechanisms that guarantee specific and efficient phosphorylation
of these sites have not been elucidated. Here, we report on three novel and
diverse protein kinase structures that reveal an exchanged activation segment
conformation. This dimeric arrangement results in an active kinase conformation
in trans, with activation segment phosphorylation sites in close proximity to
the active site of the interacting protomer. Analytical ultracentrifugation and
chemical cross-linking confirmed the presence of dimers in solution. Consensus
substrate sequences for each kinase showed that the identified activation
segment autophosphorylation sites are non-consensus substrate sites. Based on
the presented structural and functional data, a model for specific activation
segment phosphorylation at non-consensus substrate sites is proposed that is
likely to be common to other kinases from diverse subfamilies.
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