ArticleNature communications2016
Production of unstable proteins through the formation of stable core complexes.
Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Towards a phylogenetically informed approach to solving protein-protein interactions.Biochemical Society transactions · 2025Review
- The multimerization pathway of the glucocorticoid receptor.Nucleic acids research · 2025Article
- BPA: a BERT-based priority annotation strategy for assessing the rationality of aquatic algal protein sequences.Briefings in bioinformatics · 2025Article
- The HIV-1 Integrase C-Terminal Domain Induces TAR RNA Structural Changes Promoting Tat Binding.International journal of molecular sciences · 2022Article
- Oligomeric interactions maintain active-site structure in a noncooperative enzyme family.The EMBO journal · 2022Article
- Efficient production of protein complexes in mammalian cells using a poxvirus vector.PloS one · 2022Article
- Modulation of the functional association between the HIV-1 intasome and the nucleosome by histone amino-terminal tails.Retrovirology · 2017Article
Corrections and comments
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Authors and funding
6 authors.
Funding
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Abstract
Purification of proteins that participate in large transient complexes is impeded by low amounts, heterogeneity, instability and poor solubility. To circumvent these difficulties we set up a methodology that enables the production of stable complexes for structural and functional studies. This procedure is benchmarked and applied to two challenging protein families: the human steroid nuclear receptors (SNR) and the HIV-1 pre-integration complex. In the context of transcriptional regulation studies, we produce and characterize the ligand-binding domains of the glucocorticoid nuclear receptor and the oestrogen receptor beta in complex with a TIF2 (transcriptional intermediary factor 2) domain containing the three SNR-binding motifs. In the context of retroviral integration, we demonstrate the stabilization of the HIV-1 integrase by formation of complexes with partner proteins and DNA. This procedure provides a powerful research tool for structural and functional studies of proteins participating in non-covalent macromolecular complexes.
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