But small molecule therapeutics that can interact with the natural regulators of complement would be even more useful. A viral protein whose structure has been solved by Dr Barlow and colleagues may provide important clues for the design of such inhibitors. The virus has presumably pirated the gene from humans or another mammal. We can learn a lot from this protein, as it is used by the virus to protect itself against complement, and it s a really good inhibitor. We need to find out exactly how it clings onto its target.
Every cell contains a multitude of protein-synthesis factories, the tiny particles called ribosomes.
These are made as long precursor RNAs, which are processed and trimmed to get the mature RNA ready for use in the ribosome. If one of the enzymes responsible for processing rRNA is faulty, the synthesis of the ribosomes themselves is defective and the cells die as they cannot make new protein. The enzymes responsible for processing RNA are termed exonucleases or endonucleases, as they cut the RNA at the ends or the middle, respectively. Two forms of the complex have been identified one in the nucleus and one in cytoplasm which have 10 common components and an extra protein specific to each form. Professor Tollervey is already planning a plethora of new experiments to take advantage of the new proteomics equipment coming to Edinburgh.