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PDBsum entry 5dzx
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Cell adhesion
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PDB id
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5dzx
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References listed in PDB file
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Key reference
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Title
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Structural basis of diverse homophilic recognition by clustered α- And β-Protocadherins.
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Authors
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K.M.Goodman,
R.Rubinstein,
C.A.Thu,
F.Bahna,
S.Mannepalli,
G.Ahlsén,
C.Rittenhouse,
T.Maniatis,
B.Honig,
L.Shapiro.
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Ref.
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Neuron, 2016,
90,
709-723.
[DOI no: ]
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PubMed id
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Abstract
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Clustered protocadherin proteins (α-, β-, and γ-Pcdhs) provide a high level
of cell-surface diversity to individual vertebrate neurons, engaging in highly
specific homophilic interactions to mediate important roles in mammalian neural
circuit development. How Pcdhs bind homophilically through their extracellular
cadherin (EC) domains among dozens of highly similar isoforms has not been
determined. Here, we report crystal structures for extracellular regions from
four mouse Pcdh isoforms (α4, α7, β6, and β8), revealing a canonical
head-to-tail interaction mode for homophilic trans dimers comprising primary
intermolecular EC1:EC4 and EC2:EC3 interactions. A subset of trans interface
residues exhibit isoform-specific conservation, suggesting roles in recognition
specificity. Mutation of these residues, along with trans-interacting partner
residues, altered the specificities of Pcdh interactions. Together, these data
show how sequence variation among Pcdh isoforms encodes their diverse strict
homophilic recognition specificities, which are required for their key roles in
neural circuit assembly.
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