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PDBsum entry 5eqx
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Cell adhesion
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PDB id
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5eqx
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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 adhesive binding by desmocollins and desmogleins.
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Authors
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O.J.Harrison,
J.Brasch,
G.Lasso,
P.S.Katsamba,
G.Ahlsen,
B.Honig,
L.Shapiro.
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Ref.
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Proc Natl Acad Sci U S A, 2016,
113,
7160-7165.
[DOI no: ]
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PubMed id
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Abstract
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Desmosomes are intercellular adhesive junctions that impart strength to
vertebrate tissues. Their dense, ordered intercellular attachments are formed by
desmogleins (Dsgs) and desmocollins (Dscs), but the nature of trans-cellular
interactions between these specialized cadherins is unclear. Here, using
solution biophysics and coated-bead aggregation experiments, we demonstrate
family-wise heterophilic specificity: All Dsgs form adhesive dimers with all
Dscs, with affinities characteristic of each Dsg:Dsc pair. Crystal structures of
ectodomains from Dsg2 and Dsg3 and from Dsc1 and Dsc2 show binding through a
strand-swap mechanism similar to that of homophilic classical cadherins.
However, conserved charged amino acids inhibit Dsg:Dsg and Dsc:Dsc interactions
by same-charge repulsion and promote heterophilic Dsg:Dsc interactions through
opposite-charge attraction. These findings show that Dsg:Dsc heterodimers
represent the fundamental adhesive unit of desmosomes and provide a structural
framework for understanding desmosome assembly.
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