Scientists from Griffith University's Institute for Glycomics have mapped the world's first 3-D image of a protein linked to cancer, which could help in the development of medicines for the protein.
Before the discovery of this model, scientists could only guess how the structure looked. But now, scientists can see how the proteins behave, which has given them a more targeted means to create medicines that can stop the cancer protein from developing into something worse.
The model was mapped by Professor Mark von Itzsteins and a team of scientists using the X-Ray crystallography technique.
Itzstein notes that the image is so well defined that it shows both the structure of the overall protein as well as atomic-level details, Engagdet reported.
"We have successfully crystallized and determined the structure of the enzyme by X-ray crystallography, making it the first reported heparanase 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 kill the activity so that we can understand how the enzyme works," said Itzsteins, according to Science Daily. "The bacterial and human heparanase share identical substrate preference and catalytic machinery, thus enabling our heparanase structure to be used in the drug discovery process in targeting the human enzyme."
The Institute for Glycomics is the only one of its kind in Australia and only one of six in the world, according to Phys.org.
The study was published in the Nov. 2 issue of the journal Nature Chemical Biology.
