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PDBsum entry 4qmd
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Cell adhesion
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PDB id
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4qmd
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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 envoplakin plakin repeat domain
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Structure:
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Envoplakin. Chain: a, b. Synonym: 210 kda cornified envelope precursor protein, 210 kda paraneoplastic pemphigus antigen, p210. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: evpl. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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1.60Å
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R-factor:
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0.172
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R-free:
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0.205
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Authors:
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F.Mohammed,C.Al-Jassar,S.A.White,C.Fogl,M.Jeeves,T.J.Knowles, E.Odinstova,P.Rodriguez-Zamora,M.Overduin,M.Chidgey
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Key ref:
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C.Fogl
et al.
(2016).
Mechanism of intermediate filament recognition by plakin repeat domains revealed by envoplakin targeting of vimentin.
Nat Commun,
7,
10827.
PubMed id:
DOI:
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Date:
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16-Jun-14
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Release date:
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29-Jul-15
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PROCHECK
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Headers
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References
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Q92817
(EVPL_HUMAN) -
Envoplakin from Homo sapiens
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Seq:
Struc:
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2033 a.a.
193 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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DOI no:
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Nat Commun
7:10827
(2016)
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PubMed id:
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Mechanism of intermediate filament recognition by plakin repeat domains revealed by envoplakin targeting of vimentin.
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C.Fogl,
F.Mohammed,
C.Al-Jassar,
M.Jeeves,
T.J.Knowles,
P.Rodriguez-Zamora,
S.A.White,
E.Odintsova,
M.Overduin,
M.Chidgey.
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ABSTRACT
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Plakin proteins form critical connections between cell junctions and the
cytoskeleton; their disruption within epithelial and cardiac muscle cells cause
skin-blistering diseases and cardiomyopathies. Envoplakin has a single plakin
repeat domain (PRD) which recognizes intermediate filaments through an
unresolved mechanism. Herein we report the crystal structure of envoplakin's
complete PRD fold, revealing binding determinants within its electropositive
binding groove. Four of its five internal repeats recognize negatively charged
patches within vimentin via five basic determinants that are identified by
nuclear magnetic resonance spectroscopy. Mutations of the Lys1901 or Arg1914
binding determinants delocalize heterodimeric envoplakin from intracellular
vimentin and keratin filaments in cultured cells. Recognition of vimentin is
abolished when its residues Asp112 or Asp119 are mutated. The latter slot
intermediate filament rods into basic PRD domain grooves through electrosteric
complementarity in a widely applicable mechanism. Together this reveals how
plakin family members form dynamic linkages with cytoskeletal frameworks.
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Links
