2GWW Cell Adhesion, Structural Protein date May 07, 2006
title Human Vinculin (Head Domain, Vh1, Residues 1-258) In Complex With Shigella'S Ipaa Vinculin Binding Site (Residues 602-633)
authors T.Izard
compound source
Molecule: Vinculin
Chain: A
Engineered: Yes
Organism_scientific: Homo Sapiens
Organism_common: Human
Expression_system: Escherichia Coli
Expression_system_common: Bacteria

Molecule: Ipaa
Chain: B
Engineered: Yes

Organism_scientific: Shigella Flexneri
Expression_system: Escherichia Coli
Expression_system_common: Bacteria
symmetry Space Group: I 41 3 2
R_factor 0.229
crystal
cell
length a length b length c angle alpha angle beta angle gamma
151.310 151.310 151.310 90.00 90.00 90.00
method X-Ray Diffractionresolution 2.72 Å
Gene VCL (H. sapiens)
Gene
Ontology
ChainFunctionProcessComponent
A
  • actin binding
  • structural molecule activity...
  • protein binding
  • oxidoreductase activity
  • alpha-catenin binding
  • cell motility
  • cell adhesion
  • lamellipodium biogenesis
  • regulation of cell migration...
  • negative regulation of cell ...
  • apical junction assembly
  • cytoplasm
  • cytoskeleton
  • plasma membrane
  • intercellular junction
  • adherens junction
  • fascia adherens
  • focal adhesion
  • actin cytoskeleton
  • cell junction
  • cell-matrix junction
  • costamere
  • protein complex
  • B
  • actin binding
  • vinculin binding
  • pathogenesis
  • positive regulation of actin...

  • Primary referenceShigella applies molecular mimicry to subvert vinculin and invade host cells., Izard T, Tran Van Nhieu G, Bois PR, J Cell Biol. 2006 Nov 6;175(3):465-75. PMID:17088427
    Data retrieval
  • Asymmetric unit, PDB entry: [header only] [complete with coordinates] (52 Kb) [Save to disk]
  • Biological Unit Coordinates (2gww.pdb1.gz) 47 Kb
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