Kinase dead vs Active kinase and substrate interaction

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Proton Member
Proton Member
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Kinase dead vs Active kinase and substrate interaction

Postby ChristianG » Sun Sep 15, 2013 11:52 pm

Dear all,

I have a question about the interaction between a kinase dead version of a kinase and its substrates. My colleagues always told me that apparently the kinase dead version binds more tightly to a substrate than what would do the wild type, as if the kinase dead stays attached to the substrate trying to phosphorylate it (but it cannot..). Based on this idea if one immunoprecipitates the kinase dead version of a kinase, he should find more "real" substrates…Can you tell me whether this story is true? Or, better, do you know any scientific evidence about this?
I ask you this cause my colleagues do not know any…and they say is more an unwritten rule/speculation rather than a real scientific proof.

Hope you can help!



E. Coli Lysate Member
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Postby Infinity » Tue Oct 01, 2013 10:56 am

I'm not sure it is true in general. Dead kinase might not be able to phosphorylate substrate because of the mutation in catalytic site but it might not affect substrate binding. I think it might depend on which strategy is used to produce dead kinase.

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