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Novel Receptor Guides Germ Cell Transepithelial Migration in Drosophila 英文参考文献
Research Digest
Synopses of Research Articles
Structure of Aquaporin Reveals Mechanism for Transport Selectivity
Biochemists aren’t much accustomed to seeing their work in
the popular press, save for annual coverage of the Nobel prize
in chemistry.This year, Roderick MacKinnon was recognized for
working out the atomic structure of an ion channel and Peter
Agre for discovering that a major protein found in red blood cells
functions primarily as a water channel. Agre went on to establish
the family of related channels, which he named“aquaporins.’’
After fabricating and growing a recombinant form of AqpZ in
E. coli, David Savage in the Stroud group recovered the proteins
from the bacterial colonies, then puri?ed and concentrated them.
The proteins were crystallized—capturing ?ve water molecules
inside—and then analyzed by state-of-the-art high-resolution
X-ray diffraction techniques.The architecture of aquaporin Z, the
researchers report, is typical of aquaporins, with a spiral of eight
oxygens providing water-binding sites inside the channel and
amino acid side chains determining the size and
chemistry of the channel.The outer
membrane and cytoplasmic
Channel proteins have aqueous
membrane and regulate the
?ow of molecules in and
out of cells.Water passively
pours though aquaporins by
osmosis, moving from low
to high concentrations
pores that cross the cell
ends of the channel are
wider than the interior,
which is long and narrow.
of solutes. Solving
This structure con?rms
the structure of these
that aquaporin selectivity
channels provided a
arises in part from erecting
platform for exploring
a physical barrier: small
the underlying molecular
mechanisms that allow
molecules, like water, can
easily pass, but larger ones
the proteins to function as
?lters and maintain osmotic
equilibrium. Robert Stroud
and colleagues recently solved
the atomic structure of an
aquaporin (GlpF) and have
now solved the structure
of another water channel
from Escherichia coli, called
a
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