ArticleActa crystallographica. Section F, Structural biology communications2015
Crystals of the Arp2/3 complex in two new space groups with structural information about actin-related protein 2 and potential WASP binding sites.
Article in Acta crystallographica. Section F, Structural biology communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed.
- Cytochalasin B Mitigates the Inflammatory Response in Lipopolysaccharide-Induced Mastitis by Suppressing Both the ARPC3/ARPC4-Dependent Cytoskeletal Changes and the Association Between HSP70 and the NLRP3 Inflammasome.International journal of molecular sciences · 2025Article
- Cryo-EM reveals the transition of Arp2/3 complex from inactive to nucleation-competent state.Nature structural & molecular biology · 2020Article
- SPIN90 associates with mDia1 and the Arp2/3 complex to regulate cortical actin organization.Nature cell biology · 2020Article
- Single-Turnover Activation of Arp2/3 Complex by Dip1 May Balance Nucleation of Linear versus Branched Actin Filaments.Current biology : CB · 2019Article
- Structure of the nucleation-promoting factor SPIN90 bound to the actin filament nucleator Arp2/3 complex.The EMBO journal · 2018Article
- Conformational changes in Arp2/3 complex induced by ATP, WASp-VCA, and actin filaments.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Identification of Wiskott-Aldrich syndrome protein (WASP) binding sites on the branched actin filament nucleator Arp2/3 complex.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Whole Wiskott‑Aldrich syndrome protein gene deletion identified by high throughput sequencing.Molecular medicine reports · 2017Article
- Identification of an ATP-controlled allosteric switch that controls actin filament nucleation by Arp2/3 complex.Nature communications · 2016Article
- Role and structural mechanism of WASP-triggered conformational changes in branched actin filament nucleation by Arp2/3 complex.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
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Abstract
Co-crystals of the bovine Arp2/3 complex with the CA motif from N-WASP in two new space groups were analyzed by X-ray diffraction. The crystals in the orthorhombic space group P212121 contained one complex per asymmetric unit, with unit-cell parameters a = 105.48, b = 156.71, c = 177.84 Å, and diffracted to 3.9 Å resolution. The crystals in the tetragonal space group P41 contained two complexes per asymmetric unit, with unit-cell parameters a = b = 149.93, c = 265.91 Å, and diffracted to 5.0 Å resolution. The electron-density maps of both new crystal forms had densities for small segments of subdomains 1 and 2 of Arp2. Both maps had density at the binding site on Arp3 for the C-terminal EWE tripeptide from N-WASP and a binding site proposed for the C motif of N-WASP in the barbed-end groove of Arp2. The map from the tetragonal crystal form had density near the barbed end of Arp3 that may correspond to the C helix of N-WASP. The noise levels and the low resolution of the maps made the assignment of specific molecular structures for any of these CA peptides impossible.
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