ArticleThe Journal of biological chemistry2019
How metal cofactors drive dimer-dodecamer transition of the M42 aminopeptidase TmPep1050 of
Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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Who cites it
3 citing papers in PubMed, 10 citations in OpenAlex.
- Drug targeting of aminopeptidases: importance of deploying a right metal cofactor.Biophysical reviews · 2024Review
- Functional control of a 0.5 MDa TET aminopeptidase by a flexible loop revealed by MAS NMR.Nature communications · 2022Article
- Active site metals mediate an oligomeric equilibrium in Plasmodium M17 aminopeptidases.The Journal of biological chemistryArticle
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The M42 aminopeptidases are dinuclear aminopeptidases displaying a peculiar tetrahedron-shaped structure with 12 subunits. Their quaternary structure results from the self-assembly of six dimers controlled by their divalent metal ion cofactors. The oligomeric-state transition remains debated despite the structural characterization of several archaeal M42 aminopeptidases. The main bottleneck is the lack of dimer structures, hindering the understanding of structural changes occurring during the oligomerization process. We present the first dimer structure of an M42 aminopeptidase, TmPep1050 of
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