World’s First 3D Protein Image Makes History in Cancer Research

The first 3-D image of a protein linked to cancer is a historical finding that may lead to a cure for the deadly disease.


Griffith University’s Institute for Glyconomics has revealed the first 3D image of a protein linked to cancer, raising optimistic hopes for future development of a cure.


In an unprecedented historic development in technology and the fight against cancer, Griffith University’s Institute for Glycomics has determined the world’s first three-dimensional image of a protein that is linked to the spread of cancer. The 3D image, published in the journal Nature Chemical Biology, depicts a bacterial heparanase, an enzyme that breaks down sugars – which is functionally identical to a human protein that has been identified as being over-expressed in cancers.


Mark von Itzstein, Griffith University’s Director and Professor, describes the image as remarkably well defined, as it reveals the structure and atomic-level details of the protein. X-Ray crystallography was the technique used by the research team , a pioneering tool that will allow scientist to clearly see, through 3D modeling, how the enzymes functions and with that knowledge, hopefully move forward toward the development of medicines that can target and control it.


The bacterial heparanase twin of the human protein, mimics the behavior that plays a role in creating new blood vessels from pre-existing ones. This “angiogenesis” is a factor in the spread of cancer, as well as inflammation. “This research has been 10 years in the making and we will now turn our focus to developing a novel anti-cancer drug”, stressed Itzstein.


The University’s news release stated the importance of the progress, “Until now researchers from across the world have only been able to make a ‘best guess’ from computational studies of what the 3D structure of the enzyme looked like.


Itzstein said, “We have successfully crystalized and determined the structure of the enzyme by X-ray crystallography, making it the first reported hearanase X-ray crystal structure in the world. This tells us exactly where substrates bind in the catalytic domain and we explored this region by mutating certain amino acids that kills the activity so that it can be understood how the enzyme works.”


The University’s Institute for Glycomics is the only one of its kind in Australia and only one of six in the world, which has grown from “a handful of researchers to more than 180 of the best from across the world. Our research is a brave new frontier and we are making great advances towards the discovery of new drugs, vaccines, and diagnostics for significant diseases, including various cancers”, said Itzstein.


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Release ID: 96022