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Structural basis of Arpin homodimerization reveals cooperative inhibition of the Arp2/3 complex through dual-site engagement

A peer-reviewed journal article reports that Arpin forms homodimers that enable cooperative inhibition of the Arp2/3 complex by engaging two sites. The article was published by Oxford University Press on 2026-03-24.

Figure 1 Molecular structure of the ADAM17 protein. (A) Sequence and structure of ADAM17. ADAM17 protein mainly comprises five extracellular domains, a transmembrane domain, and a cytoplasmic domain. (B) The classic cysteine-switch mechanism. The conserved cysteine switch is located in the prodomain. It coordinates with Zn2+ at the catalytic site of the metalloproteinase domain to produce an inactivated enzyme (ADAM17 precursor). Once its prodomain is cleaved, the adjacent furin site (RVKR seque
Illustrative image: Figure 1 Molecular structure of the ADAM17 protein. (A) Sequence and structure of ADAM17. ADAM17 protein mainly comprises five extracellular domains, a transmembrane domain, and a cytoplasmic domain. (B) The classic cysteine-switch mechanism. The conserved cysteine switch is located in the prodomain. It coordinates with Zn2+ at the catalytic site of the metalloproteinase domain to produce an inactivated enzyme (ADAM17 precursor). Once its prodomain is cleaved, the adjacent furin site (RVKR seque — Wang K, Xuan Z, Liu X, Zheng M, Yang C and Wang H/Wikimedia Commons, CC BY 4.0

Categories: science-and-space

Generated scores

Scores are based on the cited reporting and use a 1–10 scale. Read the methodology.

Confidence
6/10
Geographic reach
1/10
Global importance
3/10
Impact magnitude
3/10
Positivity
7/10
Urgency
1/10

Why it matters

The reported structural mechanism is directly relevant to molecular research on regulation of the Arp2/3 complex.

Sources

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