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PDBsum entry 3k5s
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Structural protein
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PDB id
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3k5s
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References listed in PDB file
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Key reference
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Title
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T-Cadherin structures reveal a novel adhesive binding mechanism.
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Authors
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C.Ciatto,
F.Bahna,
N.Zampieri,
H.C.Vansteenhouse,
P.S.Katsamba,
G.Ahlsen,
O.J.Harrison,
J.Brasch,
X.Jin,
S.Posy,
J.Vendome,
B.Ranscht,
T.M.Jessell,
B.Honig,
L.Shapiro.
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Ref.
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Nat Struct Biol, 2010,
17,
339-347.
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PubMed id
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Abstract
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Vertebrate genomes encode 19 classical cadherins and about 100 nonclassical
cadherins. Adhesion by classical cadherins depends on binding interactions in
their N-terminal EC1 domains, which swap N-terminal beta-strands between partner
molecules from apposing cells. However, strand-swapping sequence signatures are
absent from nonclassical cadherins, raising the question of how these proteins
function in adhesion. Here, we show that T-cadherin, a
glycosylphosphatidylinositol (GPI)-anchored cadherin, forms dimers through an
alternative nonswapped interface near the EC1-EC2 calcium-binding sites.
Mutations within this interface ablate the adhesive capacity of T-cadherin.
These nonadhesive T-cadherin mutants also lose the ability to regulate neurite
outgrowth from T-cadherin-expressing neurons. Our findings reveal the likely
molecular architecture of the T-cadherin homophilic interface and its
requirement for axon outgrowth regulation. The adhesive binding mode used by
T-cadherin may also be used by other nonclassical cadherins.
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