Crystal Structure of Arp2/3 Complex

@article{Robinson2001CrystalSO,
  title={Crystal Structure of Arp2/3 Complex},
  author={Robert Charles Robinson and Kirsi Turbedsky and D A Kaiser and J B Marchand and Henry N. Higgs and Senyon Choe and Thomas D. Pollard},
  journal={Science},
  year={2001},
  volume={294},
  pages={1679 - 1684}
}
We determined a crystal structure of bovine Arp2/3 complex, an assembly of seven proteins that initiates actin polymerization in eukaryotic cells, at 2.0 angstrom resolution. Actin-related protein 2 (Arp2) and Arp3 are folded like actin, with distinctive surface features. Subunits ARPC2 p34 and ARPC4 p20 in the core of the complex associate through long carboxyl-terminal α helices and have similarly folded amino-terminal α/β domains. ARPC1 p40 is a seven-blade β propeller with an insertion that… 

Conformational changes in the Arp2/3 complex leading to actin nucleation

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Crystal structures of actin-related protein 2/3 complex with bound ATP or ADP.

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This work determined a high-resolution structure of the WasP-activated Arp2/3 complex at a branch junction and used biochemical, cell biological, and molecular dynamic simulations to understand the mechanism of WASP-mediated activation.

Molecular dynamics simulations of Arp2/3 complex activation.

The structural basis of actin filament branching by the Arp2/3 complex

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Arp2/3 complex is bound and activated by two WASP proteins

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