ArticleActa crystallographica. Section F, Structural biology and crystallization communications2013
Two high-resolution structures of the human E3 ubiquitin ligase Siah1.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 13 citations in OpenAlex.
- SIAH1-Mediated Ubiquitination and Degradation of TRIB3 Modulate Osteogenic and Adipogenic Differentiation.Stem cells international · 2026Article
- Deficiency of SIAH1 promotes the formation of filopodia by increasing the accumulation of FASN in liver cancer.Cell death & disease · 2024Article
- Synthesis and discovery of the first potent proteolysis targeting chimaera (PROTAC) degrader of AIMP2-DX2 as a lung cancer drug.Journal of enzyme inhibition and medicinal chemistry · 2023Article
- Structural Basis of the Interaction between Human Axin2 and SIAH1 in the Wnt/β-Catenin Signaling Pathway.Biomolecules · 2023Article
- The E3 ubiquitin ligase Sina regulates the assembly and disassembly of the synaptonemal complex in Drosophila females.PLoS genetics · 2019Article
- The SIAH E3 ubiquitin ligases promote Wnt/β-catenin signaling through mediating Wnt-induced Axin degradation.Genes & development · 2017Article
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Authors and funding
3 authors at 1 institution in 1 country.
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Abstract
Siah1 is an E3 ubiquitin ligase that contributes to proteasome-mediated degradation of multiple targets in key cellular processes and which shows promise as a therapeutic target in oncology. Structures of a truncated Siah1 bound to peptide-based inhibitors have been reported. Here, new crystallization conditions have allowed the determination of a construct encompassing dual zinc-finger subdomains and substrate-binding domains at significantly higher resolution. Although the crystals appear isomorphous, two structures present distinct states in which the spatial orientation of one zinc-finger subdomain differs with respect to the rest of the dimeric protein. Such a difference, which is indicative of conformational freedom, infers potential biological relevance related to recognition of binding partners. The crystallization conditions and improved models of Siah1 may aid future studies investigating Siah1-ligand complexes.
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