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Peter Mace, of the Otago biochemistry department, led the research, working with Australian scientists. The study's first two authors are Johannes Weijman and Dr Abhishek Kumar, of the department.
Dr Mace is ''very excited'' about the outcome of this ''fundamental biochemistry of cells'', which sheds new light on several disease processes.
The Otago-led study of a protein called apoptosis signal-regulating kinase 1 (ASK1) has just been published in PNAS.
Apoptosis is programmed cell death, which protects the rest of the body if damage to an individual cell is too great.
ASK1 and other kinases act as signalling proteins that control many aspects of cellular behaviour. Kinases put tags on to other proteins that can turn them on or off, which in turn can make a cell respond in many ways, including by dividing, dying or moving.
ASK1 also helps control how a cell responds to damage, including by pushing it towards apoptosis.
The research team determined ASK1's previously ''very little known'' molecular structure through using the Melbourne-based Australian synchrotron.
Researchers had learned a lot more about how the protein was turned on and off, which was ''important'', because in diseases such as Parkinson's, stomach cancer and melanoma there could be either ''too much of, or too little ASK1 activity''.
Kinases were ''excellent targets'' for developing new drugs because they had a ''pocket'' in their structure that such compounds could bind to.
But to develop better drugs, far more knowledge was needed, he said.