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5 December 2013 11:26 am ,
Vol. 342 ,
Dyslexia, a learning disability that hinders reading, hasn't been associated with deficits in vision, hearing, or...
Exotic, elusive, and dangerous, snakes have fascinated humankind for millennia. They can be hard to find, yet their...
Researchers have sequenced and analyzed the first two snake genomes, which represent two evolutionary extremes. The...
Snake venoms are remarkably complex mixtures that can stun or kill prey within minutes. But more and more researchers...
At age 30, Dutch biologist Freek Vonk has built up a respectable career as a snake scientist. But in his home country,...
Since arriving on the island of Guam in the 1940s, the brown tree snake ( Boiga irregularis ) has extirpated native...
An animal rights group known as the Nonhuman Rights Project filed lawsuits in three New York courts this week in an...
Researchers have been hot on the trail of the elusive Denisovans, a type of ancient human known only by their DNA and...
- 5 December 2013 11:26 am , Vol. 342 , #6163
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Detailed Look at Molecular Railway Ties
23 December 1997 7:00 pm
WASHINGTON, D.C.--Biophysicists have solved the structure of a protein that makes up the cell's internal rail system, transporting everything from proteins to DNA. The new structure, unveiled here last week at a meeting of the American Society for Cell Biology, may help researchers design better anticancer drugs and fungicides.
The protein, called tubulin, aligns into long tubular filaments that shuttle molecules through the cell and are essential for guiding chromosomes during the line dance of cell division. For years, attempts to use x-ray crystallography to determine tubulin's structure failed because the protein refused to crystallize properly.
Taking another tack, Kenneth Downing and Eva Nogales of the Lawrence Berkeley National Laboratory in California crafted a tubulin sheet just one molecule thick--a simpler task that allowed them to use an alternative technique called electron beam crystallography. They bounced very low energy electrons off the sheet from many different angles to compose a three-dimensional image. The tubulin structure will appear in the 8 January 1998 issue of Nature.
"It's a huge milestone in the cytoskeleton field," says Duke cell biologist Harold Erickson. The structure reveals how tubulin's two parts interlock and which amino acids appear to be crucial for the protein to latch onto other molecules. The structure also shows the binding site of taxol, an important anticancer drug that works by tossing up roadblocks on the microtubule highway. That information might allow researchers to design a family of microtubule disrupters.