ArticleCurrent topics in medicinal chemistry2013
Impact of quaternary structure dynamics on allosteric drug discovery.
Article in Current topics in medicinal chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 18 citations in OpenAlex.
- CADD-based discovery of novel oligomeric modulators of PKM2 with antitumor activity in aggressive human glioblastoma models.Heliyon · 2025Article
- Structural basis for the regulation of human 5,10-methylenetetrahydrofolate reductase by phosphorylation and S-adenosylmethionine inhibition.Nature communications · 2018Article
- New protein structures provide an updated understanding of phenylketonuria.Molecular genetics and metabolism · 2017Review
- Identification of Non-nucleoside Human Ribonucleotide Reductase Modulators.Journal of medicinal chemistry · 2015Article
- Probing allosteric mechanisms using native mass spectrometry.Current opinion in structural biology · 2015Review
- Compounds identified by virtual docking to a tetrameric EGFR extracellular domain can modulate Grb2 internalization.BMC cancer · 2015Article
- Allosteric targeting of receptor tyrosine kinases.Nature biotechnology · 2014Article
- ASD v2.0: updated content and novel features focusing on allosteric regulation.Nucleic acids research · 2014Article
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Abstract
The morpheein model of allosteric regulation draws attention to proteins that can exist as an equilibrium of functionally distinct assemblies where: one subunit conformation assembles into one multimer; a different subunit conformation assembles into a different multimer; and the various multimers are in a dynamic equilibrium whose position can be modulated by ligands that bind to a multimer-specific ligand binding site. The case study of porphobilinogen synthase (PBGS) illustrates how such an equilibrium holds lessons for disease mechanisms, drug discovery, understanding drug side effects, and identifying proteins wherein drug discovery efforts might focus on quaternary structure dynamics. The morpheein model of allostery has been proposed as applicable for a wide assortment of disease-associated proteins (Selwood, T., Jaffe, E., (2012) Arch. Bioch. Biophys, 519:131-143). Herein we discuss quaternary structure dynamics aspects to drug discovery for the disease-associated putative morpheeins phenylalanine hydroxylase, HIV integrase, pyruvate kinase, and tumor necrosis factor α. Also highlighted is the quaternary structure equilibrium of transthyretin and successful drug discovery efforts focused on controlling its quaternary structure dynamics.
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