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Vol. 12, Issue 6, 1765-1773, June 2001
and
*Duke University Medical Center, Department of Cell Biology,
Durham, North Carolina 27710-3709; and We have investigated the structure of the cell adhesion molecule L1
by electron microscopy. We were particularly interested in the
conformation of the four N-terminal immunoglobulin domains, because
x-ray diffraction showed that these domains are bent into a horseshoe
shape in the related molecules hemolin and axonin-1. Surprisingly,
rotary-shadowed specimens showed the molecules to be elongated, with no
indication of the horseshoe shape. However, sedimentation data
suggested that these domains of L1 were folded into a compact shape in
solution; therefore, this prompted us to look at the molecules by an
alternative technique, negative stain. The negative stain images showed
a compact shape consistent with the expected horseshoe conformation. We
speculate that in rotary shadowing the contact with the mica caused a
distortion of the protein, weakening the bonds forming the horseshoe
and permitting the molecule to extend. We have thus confirmed that the
L1 molecule is primarily in the horseshoe conformation in solution, and
we have visualized for the first time its opening into an extended
conformation. Our study resolves conflicting interpretations from
previous electron microscopy studies of L1.
W. M. Keck
Center for Collaborative Neuroscience, Rutgers University, Piscataway
New Jersey 08854-8082
Corresponding authors. E-mail
addresses: MGrumet{at}rci.rutgers.edu and H.Erickson{at}cellbio.duke.edu.
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