ArticlePloS one2013
Structure of the SCAN domain of human paternally expressed gene 3 protein.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 14 citations in OpenAlex.
- Clinical features and search for genetic determinants of postprandial hypoglycaemia.Endocrine connections · 2025Article
- Identification of sixteen novel candidate genes for late onset Parkinson's disease.Molecular neurodegeneration · 2021Article
- A functional outside-in signaling network of proteoglycans and matrix molecules regulating autophagy.Matrix biology : journal of the International Society for Matrix Biology · 2021Article
- Catabolic degradation of endothelial VEGFA via autophagy.The Journal of biological chemistry · 2020Article
- Role of the zinc finger and SCAN domain-containing transcription factors in cancer.American journal of cancer research · 2019Review
- Decorin-evoked paternally expressed gene 3 (PEG3) is an upstream regulator of the transcription factor EB (TFEB) in endothelial cell autophagy.The Journal of biological chemistry · 2017Article
- Decorin-inducible Peg3 Evokes Beclin 1-mediated Autophagy and Thrombospondin 1-mediated Angiostasis.The Journal of biological chemistry · 2017Article
- PEG3 control on the mammalian MSL complex.PloS one · 2017Article
- The Mutational Landscape of the Oncogenic MZF1 SCAN Domain in Cancer.Frontiers in molecular biosciences · 2016Article
- Two high-resolution structures of the human E3 ubiquitin ligase Siah1.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
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Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human paternally expressed gene 3 protein (PEG3) is a large multi-domain entity with diverse biological functions, including acting as a transcription factor. PEG3 contains twelve Cys2-His2 type zinc finger domains, extended regions of predicted disorder and at the N-terminus a SCAN domain. PEG3 has been identified as partner of the E3 ubiquitin-protein ligase Siah1, an association we sought to investigate. An efficient bacterial recombinant expression system of the human PEG3-SCAN domain was prepared and crystals appeared spontaneously when the protein was being concentrated after purification. The structure was determined at 1.95 Å resolution and reveals a polypeptide fold of five helices in an extended configuration. An extensive dimerization interface, using almost a quarter of the solvent accessible surface, and key salt bridge interactions explain the stability of the dimer. Comparison with other SCAN domains reveals a high degree of conservation involving residues that contribute to the dimer interface. The PEG3-SCAN domain appears to constitute an assembly block, enabling PEG3 homo- or heterodimerization to control gene expression in a combinatorial fashion.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.