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PDBsum entry 1l3w
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Cell adhesion, metal binding protein
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PDB id
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1l3w
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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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C-Cadherin ectodomain structure and implications for cell adhesion mechanisms.
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Authors
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T.J.Boggon,
J.Murray,
S.Chappuis-Flament,
E.Wong,
B.M.Gumbiner,
L.Shapiro.
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Ref.
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Science, 2002,
296,
1308-1313.
[DOI no: ]
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PubMed id
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Abstract
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Cadherins are transmembrane proteins that mediate adhesion between cells in the
solid tissues of animals. Here we present the 3.1 angstrom resolution crystal
structure of the whole, functional extracellular domain from C-cadherin, a
representative "classical" cadherin. The structure suggests a
molecular mechanism for adhesion between cells by classical cadherins, and it
provides a new framework for understanding both cis (same cell) and trans
(juxtaposed cell) cadherin interactions. The trans adhesive interface is a
twofold symmetric interaction defined by a conserved tryptophan side chain at
the membrane-distal end of a cadherin molecule from one cell, which inserts into
a hydrophobic pocket at the membrane-distal end of a cadherin molecule from the
opposing cell.
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Figure 1.
Fig. 1. (A) Stereo view of the C-cadherin ectodomain. Trp2 is
shown in CPK representation and colored purple; green spheres,
calcium ions; cyan, disulfide bonds; red, O-linked sugars; blue,
N-linked sugars. Individual cadherin-like domains are labeled
EC1 through EC5. (B) View 90° away from (A). (C) An example
region of the 3f[obs] - 2f[calc] electron density map contoured
at 2  centered
on the strand dimer interface. (D) An example of the 2 3f[obs] -
2f[calc] density seen for glycosylation sites. Images made with
the program SETOR (35).
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Figure 3.
Fig. 3. Potential cis dimerization interface. (A) Comparison of
similar interfaces seen in the crystal structures of the
C-cadherin ectodomain (this work), and two structures of a
two-domain fragment from E-cadherin in space groups P2[1] (PDB
code 1FF5) and C2 (PDB code 1EDH). EC1 and EC2 domains are
shown. Primary regions of contact include the front  sheet of
EC1 (strands C, D, and F), which interact with residues mainly
from the back sheet of EC2 (strands B, D, and E). (B) Detailed
stereo view of the cis-oriented interface. Residues that make
direct contact in the interface are labeled, and calcium ions
are shown as green spheres. Primes indicate the partner
molecule. The conserved residue Asp44 in the quasi- -helix
region is in close proximity to the EC2 to EC3 calcium-binding
region, although direct ligation of calcium ions is not
observed. Images were made with the program SETOR (35).
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The above figures are
reprinted
by permission from the AAAs:
Science
(2002,
296,
1308-1313)
copyright 2002.
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