ArticleProceedings of the National Academy of Sciences of the United States of America2021
The crystal structure of a 250-kDa heterotetrameric particle explains inhibition of sheddase meprin β by endogenous fetuin-B.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- The Role of Meprins on the Brain Extracellular Matrix and Perineuronal Nets.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026Article
- Crossing the barrier or how regulation of ovastacin controls fertilization and translates into clinical phenotypes.iScience · 2025Review
- A unique network of attack, defence and competence on the outer membrane of the periodontitis pathogenChemical science · 2023Article
- Zymogenic latency in an ∼250-million-year-old astacin metallopeptidase.Acta crystallographica. Section D, Structural biology · 2022Article
- Helical ultrastructure of the metalloprotease meprin α in complex with a small molecule inhibitor.Nature communications · 2022Article
- Dynamics of the secreted frizzled related protein Sizzled and potential implications for binding to bone morphogenetic protein-1 (BMP-1).Scientific reports · 2022Article
- Structural and evolutionary insights into astacin metallopeptidases.Frontiers in molecular biosciences · 2022Article
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5 authors.
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Abstract
Meprin β (Mβ) is a multidomain type-I membrane metallopeptidase that sheds membrane-anchored substrates, releasing their soluble forms. Fetuin-B (FB) is its only known endogenous protein inhibitor. Herein, we analyzed the interaction between the ectodomain of Mβ (MβΔC) and FB, which stabilizes the enzyme and inhibits it with subnanomolar affinity. The MβΔC:FB crystal structure reveals a ∼250-kDa, ∼160-Å polyglycosylated heterotetrameric particle with a remarkable glycan structure. Two FB moieties insert like wedges through a "CPDCP trunk" and two hairpins into the respective peptidase catalytic domains, blocking the catalytic zinc ions through an "aspartate switch" mechanism. Uniquely, the active site clefts are obstructed from subsites S
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