WELLINGTON, Oct. 9 -- A new understanding of a key protein involved in the development of blood and other cancers could lead to new treatments, according to New Zealand-led research out on Friday.

New Zealand and Australian researchers have created the first three-dimensional image of the protein, called Trib1, which plays a vital role in controlling how and when other proteins are degraded, which is essential for balancing protein levels in the cell.

Otago University researcher Dr. Peter Mace said solving the structure of Trib1 could help in developing new drugs to treat cancers such as acute myeloid leukaemia (AML), which could be caused by excess Trib1 protein driving abnormal production of white blood cells.

Trib1 was part of the protein family Tribbles, which played diverse roles in cell signalling and development, Mace said in a statement.

Tribbles were unusual types of proteins called pseudokinases, which had been described as "dead" enzymes because their structures evolved to leave them incapable of catalyzing chemical reactions.

The researchers used powerful X-ray beams 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 acted as a scaffold to bring many proteins together 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 AML," said Mace.

The researchers were interested in looking at Trib1 function in other cancers where it was overexpressed, such as prostate and breast cancer.