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Raw data used to generate the structure of cortactin bound to the Arp2/3 complex

ABSTRACT:

SUBMITTER: Roberto Dominguez

PROVIDER: EMPIAR-12055 | biostudies-other |

REPOSITORIES: biostudies-other

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Mechanism of synergistic activation of Arp2/3 complex by cortactin and WASP-family proteins.

Fregoso Fred E FE Boczkowska Malgorzata M Rebowski Grzegorz G Carman Peter J PJ van Eeuwen Trevor T Dominguez Roberto R

Nature communications 20231028 1

Cortactin coactivates Arp2/3 complex synergistically with WASP-family nucleation-promoting factors (NPFs) and stabilizes branched networks by linking Arp2/3 complex to F-actin. It is poorly understood how cortactin performs these functions. We describe the 2.89 Å resolution cryo-EM structure of cortactin's N-terminal domain (Cort<sub>1-76</sub>) bound to Arp2/3 complex. Cortactin binds Arp2/3 complex through an inverted Acidic domain (D20-V29), which targets the same site on Arp3 as the Acidic d ...[more]

PMID: 37898612

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