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TitleStructure of the p53 degradation complex from HPV16.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 1842, Year 2024
Publish dateFeb 28, 2024
AuthorsJohn C K Wang / Hannah T Baddock / Amirhossein Mafi / Ian T Foe / Matthew Bratkowski / Ting-Yu Lin / Zena D Jensvold / Magdalena Preciado López / David Stokoe / Dan Eaton / Qi Hao / Aaron H Nile /
PubMed AbstractHuman papillomavirus (HPV) is a significant contributor to the global cancer burden, and its carcinogenic activity is facilitated in part by the HPV early protein 6 (E6), which interacts with the E3- ...Human papillomavirus (HPV) is a significant contributor to the global cancer burden, and its carcinogenic activity is facilitated in part by the HPV early protein 6 (E6), which interacts with the E3-ligase E6AP, also known as UBE3A, to promote degradation of the tumor suppressor, p53. In this study, we present a single-particle cryoEM structure of the full-length E6AP protein in complex with HPV16 E6 (16E6) and p53, determined at a resolution of ~3.3 Å. Our structure reveals extensive protein-protein interactions between 16E6 and E6AP, explaining their picomolar binding affinity. These findings shed light on the molecular basis of the ternary complex, which has been pursued as a potential therapeutic target for HPV-driven cervical, anal, and oropharyngeal cancers over the last two decades. Understanding the structural and mechanistic underpinnings of this complex is crucial for developing effective therapies to combat HPV-induced cancers. Our findings may help to explain why previous attempts to disrupt this complex have failed to generate therapeutic modalities and suggest that current strategies should be reevaluated.
External linksNat Commun / PubMed:38418456 / PubMed Central
MethodsEM (single particle)
Resolution3.38 Å
Structure data

29941

8gcr

EMDB-29941, PDB-8gcr:
HPV16 E6-E6AP-p53 complex
Method: EM (single particle) / Resolution: 3.38 Å

Chemicals

ChemComp-ZN:
Unknown entry

Source
  • Escherichia coli (E. coli)
  • homo sapiens (human)
  • human papillomavirus type 16
  • escherichia coli o157:h7 (bacteria)
KeywordsVIRAL PROTEIN / Complex / HPV / ubiquitin ligase / tumor suppressor

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