The Wall Street Journal - Friday, 18 April 1997.

The research, published in today's issue of the journal Cell, is the culmination of a decade of attempts to elucidate the three-dimensional structure of gp41, one of two proteins that surround the human immunodeficiency virus, which causes AIDS. Scientists at Whitehead, a nonprofit research foundation affilitated with the Massachusetts Institute of Technology, have filed for a patent on their discovery. But they also plan to immediately post a picture of the protein on a computer data bank available to researchers around the world.

"It is our hope that people in academia and in industry will use it in whatever way they can to develop drugs that could be useful against HIV ," said Peter S. Kim, an MIT biology professor who co-authored the paper.

Knowledge of the structure of other HIV proteins has been crucial to AIDS research. In 1989, for example, scientists at Merck & Co. published the structure of HIV protease, a protein the virus needs to reproduce itself. Drugs that bind to vulnerable spots on both that protein and another protein called reverse transcriptase are the main components of new pharmaceutical cocktails that have prolonged the lives of thousands of patients.

To date, however no drugs on the market attack the so-called "envelope proteins," two large molecules that surround the virus and serve as a sort of battering ram to attack human cells and inject them with the virus. The envelope proteins had been difficult to study, mainly because scientists hadn't succeeded in making crystals of them. The crystals are needed for a technique called X-ray crystallography, in which scientists bombard a protein crystal with X-rays, then use complex mathematical formulas to deduce its structure based on how the X-rays are scattered as they exit the crystal.

The Whitehead researchers, after struggling for years to make the crystals, finally took a seemingly obvious step. They simply cut the protein in half, and made a crystal of the part they believed to be most active. What they found was "striking," says Dr. Kim. Near the center of the protein was an unusually deep cavity. Researchers believe that another part of the protein fits into it like a ball into a socket.

"This is very exciting news. I congratulate the researchers on a very big achievement," said Dr. Krzysztof Appelt, an X-ray crystallographer who is a senior research fellow at Agouron Pharmaceuticals Inc. of La Jolla, Calif. He predicts there will be "a lot of interest" in using the information to design a drug, but cautions that it could be two or three years before one is available for testing in humans.

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