Dr Mace said the discovery in the early 2000s of a range of pseudokinases persisting in cells was initially puzzling, until it became clear that they were now performing other important non-enzymatic functions.
The researchers used powerful X-ray beams at the Australian Synchrotron to obtain the detailed three-dimensional images of Trib1, revealing that its structure had been hugely contorted compared to related proteins that do function as catalysts.
Instead of driving chemical reactions Trib1 acts as a scaffold to bring many proteins together, and the team discovered how Trib1 "recruits" specific proteins to be degraded.
"As well as explaining how Trib1 functions, our research into its structure could help us design novel therapeutic agents to block its overproduction in acute myeloid leukaemia (AML)," Dr Mace said.
AML is a particularly aggressive cancer typified by an increased number of abnormal white blood cells, called myeloid cells, and kills around half of children diagnosed with it.
In adolescent patients, this rate is even higher.
Beyond AML, the researchers were interested in looking at Trib1 function in other cancers where it is overexpressed.
"There is already some evidence that Trib1 plays a role in prostate cancer but this is fairly new ground so we have a lot to learn."
In collaboration with Department of Biochemistry colleague Dr Anita Dunbier, the team is investigating the role of Trib1 in breast cancer.
The newly-published research, featured today in the international journal Structure, was supported by the Health Research Council of New Zealand, the New Zealand government, the Australian Cancer Research Foundation, the Australian National Health and Medical Research Council and the Victorian Government Operational Infrastructure Support Program.
