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PDBsum entry 2a4c
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Cell adhesion
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PDB id
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2a4c
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References listed in PDB file
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Key reference
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Title
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Type ii cadherin ectodomain structures: implications for classical cadherin specificity.
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Authors
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S.D.Patel,
C.Ciatto,
C.P.Chen,
F.Bahna,
M.Rajebhosale,
N.Arkus,
I.Schieren,
T.M.Jessell,
B.Honig,
S.R.Price,
L.Shapiro.
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Ref.
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Cell, 2006,
124,
1255-1268.
[DOI no: ]
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PubMed id
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Abstract
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Type I and II classical cadherins help to determine the adhesive specificities
of animal cells. Crystal-structure determination of ectodomain regions from
three type II cadherins reveals adhesive dimers formed by exchange of N-terminal
beta strands between partner extracellular cadherin-1 (EC1) domains. These
interfaces have two conserved tryptophan side chains that anchor each swapped
strand, compared with one in type I cadherins, and include large hydrophobic
regions unique to type II interfaces. The EC1 domains of type I and type II
cadherins appear to encode cell adhesive specificity in vitro. Moreover,
perturbation of motor neuron segregation with chimeric cadherins depends on EC1
domain identity, suggesting that this region, which includes the structurally
defined adhesive interface, encodes type II cadherin functional specificity in
vivo.
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Figure 1.
Figure 1. Structure of Multidomain Type II Cadherin
Fragments
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Figure 4.
Figure 4. Comparison of Binding Surfaces for Type II
Cadherins and Type I Cadherins
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The above figures are
reprinted
by permission from Cell Press:
Cell
(2006,
124,
1255-1268)
copyright 2006.
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