IN THIS ISSUE . . .
March 21, 2006
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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. To read additional news items, visit NIGMS
Cool Image: Beaded Bacteriophage
This sculpture made of purple and clear glass beads depicts
bacteriophage φX174, a virus that infects bacteria.
It rests on a surface that portrays an adaptive landscape,
a conceptual visualization. The ridges represent the gene
combinations associated with the greatest fitness levels
of the virus, as measured by how quickly the virus can reproduce
itself. φX174 is an important model system for studies
of viral evolution because its genome can readily be sequenced
as it evolves under defined laboratory conditions. Courtesy
of Holly Wichman, an evolutionary biologist at the University
of Idaho. (Sculpture by Wichman; surface by A. Johnston,
an undergraduate student in landscape architecture; and
photo by J. Palmersheim.)
lab home page
Computer Models Could Speed Drug Discovery
structure of a receptor for dopamine, a neurotransmitter.
Courtesy of Jeffrey Skolnick, Yang Zhang, and Mark
A team led by systems biologist Jeffrey Skolnick of the Georgia
Institute of Technology has created computer models of more
than 900 cell receptors from a class of proteins targeted
by many drugs. Because these G protein-coupled receptors tend
to fall apart outside their cellular environment, researchers
have determined very few of their structures experimentally.
While the computer-generated structures don’t capture
all the details of the actual receptors, the models may speed
drug discovery by helping researchers study how different
compounds interact with cellular targets.
abstract (from the February 17, 2006, issue of PLoS Computational
Common Mechanism May Underlie Neurodegenerative
worm expressing a protein prone to clumping that fluoresces
green (right), and a related protein that does not
Clumps of misfolded and damaged proteins that destroy brain
cells are a hallmark of neurodegenerative diseases. But explanations
for what causes cell death in Alzheimer’s, Parkinson’s,
Huntington’s, and other diseases vary widely, leading
scientists to question the connection among the brain disorders.
A new study led by cell biologist Richard Morimoto of Northwestern
University offers evidence that a common mechanism may underlie
these diseases. When the research team introduced a protein
prone to clumping into the roundworm C. elegans,
they found that unrelated, semi-stable proteins in the cells
lost their ability to fold and, as a result, function properly.
The researchers suggest that this loss of function would interfere
with many cellular processes, possibly explaining the cell
damage and death associated with neurodegenerative diseases.
Lab home page
abstract (from the February 9, 2006, issue of Science)
Cracking Open an Anti-Cocaine Molecule
of an antibody molecule (light blue surface) bound
to cocaine (colored sticks). Courtesy of Ian Wilson
and Xueyong Zhu. This work was co-funded by the
National Institute on Drug Abuse at NIH.
Cocaine abuse remains a major public health problem. While
no effective medication exists to treat cocaine addiction
and overdose, some molecules have shown promise in animal
studies. A research team led by structural biologist Ian
Wilson of the Scripps Research Institute has now revealed
the inner workings of one such molecule—an antibody
designed in the laboratory to quickly sop up and destroy
cocaine before it reaches the brain. The scientists used
X-ray crystallography to visualize molecular snapshots of
the antibody in action. The study reveals specific ways
to modify the antibody molecule to make it degrade cocaine
more efficiently. The eventual goal is to design a medication
to safely and effectively treat cocaine abuse.
lab home page
abstract (from the February 2006 issue of Structure)
Profiles in Discovery: Proteins and Viruses
Kelleher (top) and Agbandje-McKenna
The quest for new knowledge to improve health involves
thousands of NIGMS-funded scientists working at the cutting
edge of biomedical research. Among them is chemical biologist
Neil Kelleher of the University of Illinois in Urbana-Champaign,
who uses an enormous magnet and sophisticated computer tools
to analyze proteins. Read about his work in “The Humpty
Dumpty Dilemma,” appearing in the March 2006 issue
of Findings. In the same issue, go on “Viral
Voyages” with structural biologist Mavis Agbandje-McKenna,
who began life in a war-torn Nigerian village. Now at the
University of Florida, she studies how harmless viruses
can turn deadly with just a few genetic changes.
Humpty Dumpty Dilemma