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TitleHigh-Resolution Imaging of Human Cancer Proteins Using Microprocessor Materials.
Journal, issue, pagesChembiochem, Vol. 23, Issue 17, Page e202200310, Year 2022
Publish dateSep 5, 2022
AuthorsMaria J Solares / G M Jonaid / William Y Luqiu / Samantha Berry / Janki Khadela / Yanping Liang / Madison C Evans / Kevin J Pridham / William J Dearnaley / Zhi Sheng / Deborah F Kelly /
PubMed AbstractMutations in tumor suppressor genes, such as Tumor Protein 53 (TP53), are heavily implicated in aggressive cancers giving rise to gain- and loss-of-function phenotypes. While individual domains of ...Mutations in tumor suppressor genes, such as Tumor Protein 53 (TP53), are heavily implicated in aggressive cancers giving rise to gain- and loss-of-function phenotypes. While individual domains of the p53 protein have been studied extensively, structural information for full-length p53 remains incomplete. Functionalized microprocessor chips (microchips) with properties amenable to electron microscopy permitted us to visualize complete p53 assemblies for the first time. The new structures revealed p53 in an inactive dimeric state independent of DNA binding. Residues located at the protein-protein interface corresponded with modification sites in cancer-related hot spots. Changes in these regions may amplify the toxic effects of clinical mutations. Taken together, these results contribute advances in technology and imaging approaches to decode native protein models in different states of activation.
External linksChembiochem / PubMed:35789183 / PubMed Central
MethodsEM (single particle)
Resolution4.2 - 5.0 Å
Structure data

28816

8f2h

EMDB-28816, PDB-8f2h:
Wild type P53 dimer structure from human cancer cells
Method: EM (single particle) / Resolution: 4.2 Å

28817

8f2i

EMDB-28817, PDB-8f2i:
P53 monomer structure
Method: EM (single particle) / Resolution: 5.0 Å

Source
  • homo sapiens (human)
KeywordsANTITUMOR PROTEIN / cancer / tumor suppressor / cell cycle / apoptosis / DNA repair

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