HIV key enzyme structure is determined

HIV key enzyme structure is determined

LONDON - U.S. and British scientists say they have determined the three-dimensional structure of a critical enzyme found in HIV and other retroviruses. The study's lead author, Dr Peter Cherepanov of Imperial College London, said the precise structure of the enzyme called "integrase" was determined by growing a crystal using integrase from a retrovirus called the Prototype Foamy Virus that scientists believe is very similar to the human immunodeficiency virus. Growing the crystal required 40,000 trials during four years of effort by researchers from Imperial College and Harvard University.
Cherepanov said: "It is a truly amazing story. When we started out, we knew that the project was very difficult, and that many tricks had already been tried and given up by others long ago. … Despite initially painstakingly slow progress and very many failed attempts, we did not give up and our effort was finally rewarded." Researchers determined the molecular structure of the crystal with X-ray diffraction data from a synchrotron at the Diamond Light Source in South Oxfordshire. The investigators said their findings will help scientists better understand how existing drugs that inhibit integrase work, how to improve them and how to stop the human immunodeficiency virus from developing resistance to them.
The study appeared in the Jan. 31 edition of the journal Nature.

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