ArticleBiochemistry2019
Crystal Structures and Nuclear Magnetic Resonance Studies of the Apo Form of the c-MYC:MAX bHLHZip Complex Reveal a Helical Basic Region in the Absence of DNA.
Article in Biochemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 64 citations in OpenAlex.
- Targeting the MYCN interaction network in neuroblastoma.Bioscience reports · 2026Review
- Probing the Structural Dynamics of the Unbound MAX Protein: Insights from Well-Tempered Metadynamics.Journal of chemical information and modeling · 2026Article
- Multiplex mapping of protein-protein interaction interfaces.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Multiplex mapping of protein-protein interaction interfaces.bioRxiv : the preprint server for biology · 2025Article
- c-Myc promotes metabolic reprogramming in pulmonary hypertension via the stimulation of glutaminolysis and the reductive tricarboxylic acid cycle.Redox biology · 2025Article
- Discovery of a Pyrazolopyridinone-Based MYC Inhibitor That Selectively Engages Intracellular c-MYC and Disrupts MYC-MAX Heterodimerization.Journal of medicinal chemistry · 2025Article
- Structural information in therapeutic peptides: Emerging applications in biomedicine.FEBS open bio · 2025Review
- Exploring the dynamics and interactions of the N-myc transactivation domain through solution nuclear magnetic resonance spectroscopy.The Biochemical journal · 2024Article
- A druggable conformational switch in the c-MYC transactivation domain.Nature communications · 2024Article
- Unraveling the Behavior of Intrinsically Disordered Protein c-Myc: A Study Utilizing Gaussian-Accelerated Molecular Dynamics.ACS omega · 2024Article
- A recurrent de novo MAX p.Arg60Gln variant causes a syndromic overgrowth disorder through differential expression of c-Myc target genes.American journal of human genetics · 2024Article
- EBF1, PAX5, and MYC: regulation on B cell development and association with hematologic neoplasms.Frontiers in immunology · 2024Review
- NMR-identification of the interaction between BRCA1 and the intrinsically disordered monomer of the Myc-associated factor X.Protein science : a publication of the Protein Society · 2024Article
- AnMini reviews in medicinal chemistry · 2024Article
- Nilotinib: Disrupting the MYC-MAX Heterocomplex.Bioinformatics and biology insights · 2024Article
- Manipulating Myc for reparative regeneration.Frontiers in cell and developmental biology · 2024Review
- Visualizing single-molecule conformational transition and binding dynamics of intrinsically disordered proteins.Nature communications · 2023Article
- Myc beyond Cancer: Regulation of Mammalian Tissue Regeneration.Pathophysiology : the official journal of the International Society for Pathophysiology · 2023Review
- Modes of Action of a Novel c-MYC Inhibiting 1,2,4-Oxadiazole Derivative in Leukemia and Breast Cancer Cells.Molecules (Basel, Switzerland) · 2023Article
- RUNX3 inactivates oncogenic MYC through disruption of MYC/MAX complex and subsequent recruitment of GSK3β-FBXW7 cascade.Communications biology · 2023Article
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
The c-MYC transcription factor is a master regulator of cell growth and proliferation and is an established target for cancer therapy. This basic helix-loop-helix Zip protein forms a heterodimer with its obligatory partner MAX, which binds to DNA via the basic region. Considerable research efforts are focused on targeting the heterodimerization interface and the interaction of the complex with DNA. The only available crystal structure is that of a c-MYC:MAX complex artificially tethered by an engineered disulfide linker and prebound to DNA. We have carried out a detailed structural analysis of the apo form of the c-MYC:MAX complex, with no artificial linker, both in solution using nuclear magnetic resonance (NMR) spectroscopy and by X-ray crystallography. We have obtained crystal structures in three different crystal forms, with resolutions between 1.35 and 2.2 Å, that show extensive helical structure in the basic region. Determination of the α-helical propensity using NMR chemical shift analysis shows that the basic region of c-MYC and, to a lesser extent, that of MAX populate helical conformations. We have also assigned the NMR spectra of the c-MYC basic helix-loop-helix Zip motif in the absence of MAX and showed that the basic region has an intrinsic helical propensity even in the absence of its dimerization partner. The presence of helical structure in the basic regions in the absence of DNA suggests that the molecular recognition occurs via a conformational selection rather than an induced fit. Our work provides both insight into the mechanism of DNA binding and structural information to aid in the development of MYC inhibitors.
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