 |
PDBsum entry 3jz7
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Cell adhesion
|
PDB id
|
|
|
|
3jz7
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
The coxsackievirus-Adenovirus receptor reveals complex homophilic and heterophilic interactions on neural cells.
|
|
|
Authors
|
|
C.Patzke,
K.E.Max,
J.Behlke,
J.Schreiber,
H.Schmidt,
A.A.Dorner,
S.Kröger,
M.Henning,
A.Otto,
U.Heinemann,
F.G.Rathjen.
|
|
|
Ref.
|
|
J Neurosci, 2010,
30,
2897-2910.
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
The coxsackievirus-adenovirus receptor (CAR) is a member of the Ig superfamily
strongly expressed in the developing nervous system. Our histological
investigations during development reveal an initial uniform distribution of CAR
on all neural cells with a concentration on membranes that face the margins of
the nervous system (e.g., the basal laminae and the ventricular side). At more
advanced stages, CAR becomes downregulated and restricted to specific regions
including areas rich in axonal and dendritic surfaces. To study the function of
CAR on neural cells, we used the fiber knob of the adenovirus, extracellular CAR
domains, blocking antibodies to CAR, as well as CAR-deficient neural cells.
Blocking antibodies were found to inhibit neurite extension in retina organ and
retinal explant cultures, whereas the application of the recombinant fiber knob
of the adenovirus subtype Ad2 or extracellular CAR domains promoted neurite
extension and adhesion to extracellular matrices. We observed a promiscuous
interaction of CAR with extracellular matrix glycoproteins, which was deduced
from analytical ultracentrifugation experiments, affinity chromatography, and
adhesion assays. The membrane proximal Ig domain of CAR, termed D2, was found to
bind to a fibronectin fragment, including the heparin-binding domain 2, which
promotes neurite extension of wild type, but not of CAR-deficient neural cells.
In contrast to heterophilic interactions, homophilic association of CAR involves
both Ig domains, as was revealed by ultracentrifugation, chemical cross-linking,
and adhesion studies. The results of these functional and binding studies are
correlated to a U-shaped homodimer of the complete extracellular domains of CAR
detected by x-ray crystallography.
|
|
|
|
|
|
|
