ArticleActa crystallographica. Section F, Structural biology communications2019
Noncovalent structure of SENP1 in complex with SUMO2.
Article in Acta crystallographica. Section F, Structural biology communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- SENP1 prevents steatohepatitis by suppressing RIPK1-driven apoptosis and inflammation.Nature communications · 2022Article
- Hinokiflavone and Related C-O-C-Type Biflavonoids as Anti-cancer Compounds: Properties and Mechanism of Action.Natural products and bioprospecting · 2021Review
- Plasma Exosome-Derived SENP1 May Be a Potential Prognostic Predictor for Melanoma.Frontiers in oncology · 2021Article
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1 author.
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Abstract
SUMOylation is a post-translational modification in which a small ubiquitin-like molecule (SUMO) is appended to substrate proteins and is known to influence myriads of biological processes. A delicate interplay between several families of SUMOylation proteins and their substrates ensures the proper level of SUMOylation required for normal cell function. Among the SUMO proteins, SUMO2 is known to form mono-SUMOylated proteins and engage in poly-SUMO chain formation, while sentrin-specific protease 1 (SENP1) is a key enzyme in regulating both events. Determination of the SENP1-SUMO2 interaction is therefore necessary to better understand SUMOylation. In this regard, the current paper reports the noncovalent structure of SENP1 in complex with SUMO2, which was refined to a resolution of 2.62 Å with R and R
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