The National Institute of General Medical Sciences (NIGMS), one of the National Institutes of Health, supports all research featured in this digest. Although only the lead scientists are named, coworkers and other collaborators also contributed to the findings.
In This Issue... April 21, 2011
David Goodsell • RCSB Protein Data BankIf we can visualize a protein's shape, we can learn much more about how it functions and how we might block its activity. This was the guiding principle behind an NIH initiative launched 25 years ago to spur the discovery of HIV-related protein structures. Structures produced through the program have helped paint this detailed picture of the virus and have led to some important classes of drugs to treat the infection. Click on image to explore the structures of HIV. Read more...
Craig Montell • Johns Hopkins University
At one time, researchers believed that the protein rhodopsin functioned solely as a receptor for light in the eye. Now they know it also helps fruit fly larvae sense temperature. Without rhodopsin, fly larvae can avoid areas that are too hot or cold, but they cannot detect temperature variations within their comfort zone (64 to 75 degrees Fahrenheit). The research may shed light on how other animals—including people—sense temperature. Read more...
Caption: Fruit fly retina showing light-sensing protein rhodopsin-5
(blue) and rhodopsin-6 (red). Credit: Hermann Steller, Rockefeller
University. High res.
image (JPG, 50KB)
Brian Paegel • Scripps Research Institute, Florida campus
Cell membranes: They surround every cell in your body, encase all your organelles and intrigue researchers as potential drug delivery devices. But they've been hard to mass produce. Now, a new process driven by a microfluidic circuit lets scientists create synthetic membranes in an assembly-line fashion. The lab-made membranes are lipid bilayers, just like natural cell membranes, and can even include inserted proteins. The work will help scientists better understand biological cell membranes and could advance efforts to use membranes therapeutically. Read more...
Caption: A new device acts as a microscopic assembly line to
synthesize cell membranes. High
res. image (JPG, 34KB)
Erica Larschan • Brown University
Men have one X chromosome and women have two. To even things
out, men must ramp up the activity of their X chromosome. Scientists
recently figured out how it's done—at least in fruit flies. In
the males, the molecular machinery that "reads" and transcribes
DNA operates faster and travels further on X chromosome genes
than on other chromosomes. A cluster of proteins called MSL is
responsible for squeezing out this extra effort. MSL, which stands
for "male-specific lethal," acts like a power tool custom-made
for the X chromosome. Read
Caption: The male-specific protein complex (red) homes in on the X chromosome (blue) to ramp up its activity. High res. image (JPG, 60KB)
Ray Stevens • Scripps Research Institute
Our bodies sense and respond to caffeine the same way they do
to fragrances, light and other stimuli—by tweaking a molecule
called a G-protein coupled receptor (GPCR). Scientists recently
determined the detailed, 3-D structure of an active caffeine receptor.
The new structure is teaching many lessons about the large family
of GPCRs, which are the targets of many drugs, including those
that treat allergies, heart disease and Parkinson's. The research
could inform the design of new drugs for a wide range of diseases.
Caption: New structure suggests GPCR dynamics. Credit: Stevens Laboratory. High res. image (JPG, 25KB)
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