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PDBsum entry 5erp
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Cell adhesion
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PDB id
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5erp
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PDB id:
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| Name: |
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Cell adhesion
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Title:
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Crystal structure of human desmocollin-2 ectodomain fragment ec2-5
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Structure:
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Desmocollin-2. Chain: a, b. Fragment: unp residues 236-680. Synonym: cadherin family member 2,desmocollin-3,desmosomal glycoprotein ii,desmosomal glycoprotein iii. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: dsc2, cdhf2, dsc3. Expressed in: homo sapiens. Expression_system_taxid: 9606. Expression_system_cell_line: hek293
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Resolution:
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2.70Å
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R-factor:
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0.225
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R-free:
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0.262
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Authors:
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O.J.Harrison,J.Brasch,L.Shapiro
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Key ref:
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O.J.Harrison
et al.
(2016).
Structural basis of adhesive binding by desmocollins and desmogleins.
Proc Natl Acad Sci U S A,
113,
7160-7165.
PubMed id:
DOI:
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Date:
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14-Nov-15
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Release date:
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15-Jun-16
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PROCHECK
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Headers
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References
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Q02487
(DSC2_HUMAN) -
Desmocollin-2 from Homo sapiens
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Seq:
Struc:
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901 a.a.
443 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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DOI no:
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Proc Natl Acad Sci U S A
113:7160-7165
(2016)
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PubMed id:
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Structural basis of adhesive binding by desmocollins and desmogleins.
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O.J.Harrison,
J.Brasch,
G.Lasso,
P.S.Katsamba,
G.Ahlsen,
B.Honig,
L.Shapiro.
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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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Links
