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

Jie-Oh Lee, Alicia A. Russo and Nikola P. Pavletich ()
Additional contact information
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

Nature, 1998, vol. 391, issue 6670, 859-865

Abstract: 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.

Date: 1998
References: Add references at CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/36038 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:391:y:1998:i:6670:d:10.1038_36038

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/36038

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().