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PDBsum entry 1q1p
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Cell adhesion
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PDB id
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1q1p
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Proteolytic e-Cadherin activation followed by solution nmr and X-Ray crystallography.
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Authors
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D.Häussinger,
T.Ahrens,
T.Aberle,
J.Engel,
J.Stetefeld,
S.Grzesiek.
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Ref.
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EMBO J, 2004,
23,
1699-1708.
[DOI no: ]
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PubMed id
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Abstract
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Cellular adhesion by classical cadherins depends critically on the exact
proteolytic removal of their N-terminal prosequences. In this combined solution
NMR and X-ray crystallographic study, the consequences of propeptide cleavage of
an epithelial cadherin construct (domains 1 and 2) were followed at atomic
level. At low protein concentration, the N-terminal processing induces docking
of the tryptophan-2 side-chain into a binding pocket on the same molecule. At
high concentration, cleavage induces dimerization (KD=0.72 mM, k(off)=0.7 s(-1))
and concomitant intermolecular exchange of the betaA-strands and the
tryptophan-2 side-chains. Thus, the cleavage represents the switch from a
nonadhesive to the functional form of cadherin.
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Figure 1.
Figure 1 Schematic representation of prodomain -CAD1 domain
boundaries of wild-type murine E-cadherin and E-cadherin
constructs used in this study. The cleavage site of the
prodomain in the wild-type protein is indicated by a black
arrow. In HisXa-ECAD12, this cleavage site is mimicked by the
factor Xa cleavage sequence IEGR (gray arrow).
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Figure 7.
Figure 7 Comparison of the ECAD12, M-ECAD12, and CCAD1 -5
crystal structures. The interacting monomers are shown in blue
and yellow with their respective N-termini in red and green. The
W2 residue is shown as space-fill. For better comparison, the
blue CAD12 domains are shown in the same orientation for all
three structures. Calcium atoms are indicated in magenta.
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The above figures are
reprinted
from an Open Access publication published by Macmillan Publishers Ltd:
EMBO J
(2004,
23,
1699-1708)
copyright 2004.
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