Structure of the retinoblastoma tumour-suppressor pocket domain bound to a peptide from HPV E7 Journal Article
| Authors: | Lee, J. O.; Russo, A. A.; Pavletich, N. P. |
| Article Title: | Structure of the retinoblastoma tumour-suppressor pocket domain bound to a peptide from HPV E7 |
| Abstract: | The pocket domain of the retinoblastoma (Rb) tumour suppressor is central to Rb function, and to 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. |
| Keywords: | oncoprotein; protein conformation; protein domain; neoplasms; protein binding; retinoblastoma; phosphorylation; tumor suppressor gene; amino acid sequence; conserved sequence; molecular sequence data; recombinant proteins; binding site; crystal structure; models, molecular; crystallography, x-ray; binding sites; cycline; protein folding; cyclins; cyclin a; cyclin dependent kinase; retinoblastoma protein; wart virus; oncogene proteins, viral; human papilloma virus; chicken ovalbumin upstream promoter transcription factor; humans; priority journal; article; gallus gallus; human papillomavirus types |
| Journal Title: | Nature |
| Volume: | 391 |
| Issue: | 6670 |
| ISSN: | 0028-0836 |
| Publisher: | Nature Publishing Group |
| Date Published: | 1998-02-26 |
| Start Page: | 859 |
| End Page: | 865 |
| Language: | English |
| DOI: | 10.1038/36038 |
| PUBMED: | 9495340 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | Article -- Export Date: 12 December 2016 -- Source: Scopus |
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