ArticleProtein science : a publication of the Protein Society2025
Templated trimerization of the phage L decoration protein on capsids.
Article in Protein science : a publication of the Protein Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed.
- Reversible Assembly of Virus-Like Particles (VLPs) into Higher-Order Structures Controlled by Oxidation and Reduction of Linker Protein.ACS applied bio materials · 2026Article
- Templated trimerization of the phage L decoration protein on capsids.Protein science : a publication of the Protein Society · 2025Article
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5 authors.
Funding
Abstract
The 134-residue phage L decoration protein (Dec) forms a capsid-stabilizing homotrimer that has an asymmetric tripod-like structure when bound to phage L capsids. The N-termini of the trimer subunits consist of spatially separated globular OB-fold domains that interact with the virions of phage L or the related phage P22. The C-termini of the trimer form a spike structure that accounts for nearly all the interactions that stabilize the trimer. A Dec mutant with the spike residues 99-134 deleted (Dec
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Registered trials
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