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

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 consented 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.
Publisher
MACMILLAN MAGAZINES LTD
Issue Date
1998-02
Language
ENG
Keywords

ONCOGENIC POINT MUTATIONS; LARGE T-ANTIGEN; GENE-PRODUCT; CELL-CYCLE; INCOMPLETE PENETRANCE; SUSCEPTIBILITY GENE; COMPLEX-FORMATION; ADENOVIRUS E1A; RB GENE; PROTEIN

Citation

NATURE, v.391, no.6670, pp.859 - 865

ISSN
0028-0836
URI
http://hdl.handle.net/10203/75192
Appears in Collection
CH-Journal Papers(저널논문)
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