Crystal Structure of Arp2/3 Complex

@article{Robinson2001CrystalSO,
  title={Crystal Structure of Arp2/3 Complex},
  author={R. Robinson and K. Turbedsky and D. Kaiser and J. Marchand and H. Higgs and S. Choe and T. 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… Expand
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References

SHOWING 1-10 OF 67 REFERENCES
Structure and function of the Arp2/3 complex.
The interaction of Arp2/3 complex with actin: nucleation, high affinity pointed end capping, and formation of branching networks of filaments.
Activation of the Arp2/3 Complex by the Listeria ActA Protein
...
1
2
3
4
5
...