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Structure of the retinoblastoma tumour-suppressor pocket domain bound to a peptide from HPV E7

Author

Listed:
  • Jie-Oh Lee

    (Howard Hughes Medical Institute, Memorial Sloan-Kettering Cancer Center)

  • Alicia A. Russo

    (Cellular Biochemistry and Biophysics Program)

  • Nikola P. Pavletich

    (Howard Hughes Medical Institute, Memorial Sloan-Kettering Cancer Center)

Abstract

The pocket domain of the retinoblastoma (Rb) tumour suppressor is central to Rb function, and is frequently inactivated by the binding of the human papilloma virus E7 oncoprotein in cervical cancer. The crystal structure of the Rb pocket bound to a nine-residue E7 peptide containing the LxCxE motif, shared by other Rb-binding viral and cellular proteins, shows that the LxCxE peptide binds a highly conserved groove on the B-box portion of the pocket; the A-box portion appears to be required for the stable folding of the B box. Also highly conserved is the extensive A–B interface, suggesting that it may be an additional protein-binding site. The A and B boxes each contain the cyclin-fold structural motif, with the LxCxE-binding site on the B-box cyclin fold being similar to a Cdk2-binding site of cyclin A and to a TBP-binding site of TFIIB.

Suggested Citation

  • Jie-Oh Lee & Alicia A. Russo & Nikola P. Pavletich, 1998. "Structure of the retinoblastoma tumour-suppressor pocket domain bound to a peptide from HPV E7," Nature, Nature, vol. 391(6670), pages 859-865, February.
    • Handle: RePEc:nat:nature:v:391:y:1998:i:6670:d:10.1038_36038
    DOI: 10.1038/36038
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    1. Filip Mihalič & Leandro Simonetti & Girolamo Giudice & Marie Rubin Sander & Richard Lindqvist & Marie Berit Akpiroro Peters & Caroline Benz & Eszter Kassa & Dilip Badgujar & Raviteja Inturi & Muhammad, 2023. "Large-scale phage-based screening reveals extensive pan-viral mimicry of host short linear motifs," Nature Communications, Nature, vol. 14(1), pages 1-20, December.

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