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PDBsum entry 4zpq
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Cell adhesion
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PDB id
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4zpq
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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 protocadherin gamma c5 ec1-3
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Structure:
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Mcg133388, isoform cra_f. Chain: a, b, c. Fragment: unp residues 30-345. Synonym: pcdhgc5 protein,protein pcdhgc5,protocadherin gamma c-v, protocadherin gamma c5,protocadherin gamma subfamily c,5. Engineered: yes
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Source:
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Mus musculus. Mouse. Organism_taxid: 10090. Gene: pcdhgc5, mcg_133388. Expressed in: homo sapiens. Expression_system_taxid: 9606. Expression_system_cell_line: hek293
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Resolution:
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3.10Å
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R-factor:
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0.217
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R-free:
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0.252
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Authors:
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H.N.Wolcott,K.M.Goodman,F.Bahna,S.Mannepalli,L.Shapiro
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Key ref:
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R.Rubinstein
et al.
(2015).
Molecular logic of neuronal self-recognition through protocadherin domain interactions.
Cell,
163,
629-642.
PubMed id:
DOI:
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Date:
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08-May-15
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Release date:
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28-Oct-15
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PROCHECK
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Headers
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References
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Q91XW9
(Q91XW9_MOUSE) -
Pcdhgc5 protein from Mus musculus
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Seq:
Struc:
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944 a.a.
315 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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Cell
163:629-642
(2015)
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PubMed id:
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Molecular logic of neuronal self-recognition through protocadherin domain interactions.
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R.Rubinstein,
C.A.Thu,
K.M.Goodman,
H.N.Wolcott,
F.Bahna,
S.Mannepalli,
G.Ahlsen,
M.Chevee,
A.Halim,
H.Clausen,
T.Maniatis,
L.Shapiro,
B.Honig.
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ABSTRACT
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Self-avoidance, a process preventing interactions of axons and dendrites from
the same neuron during development, is mediated in vertebrates through the
stochastic single-neuron expression of clustered protocadherin protein isoforms.
Extracellular cadherin (EC) domains mediate isoform-specific homophilic binding
between cells, conferring cell recognition through a poorly understood
mechanism. Here, we report crystal structures for the EC1-EC3 domain regions
from four protocadherin isoforms representing the α, β, and γ subfamilies.
All are rod shaped and monomeric in solution. Biophysical measurements, cell
aggregation assays, and computational docking reveal that trans binding between
cells depends on the EC1-EC4 domains, which interact in an antiparallel
orientation. We also show that the EC6 domains are required for the formation of
cis-dimers. Overall, our results are consistent with a model in which
protocadherin cis-dimers engage in a head-to-tail interaction between EC1-EC4
domains from apposed cell surfaces, possibly forming a zipper-like protein
assembly, and thus providing a size-dependent self-recognition mechanism.
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