2R7G

Structure of the retinoblastoma protein pocket domain in complex with adenovirus E1A CR1 domain

Summary for 2R7G

• Entry DOI: 10.2210/pdb2r7g/pdb
• Descriptor: Retinoblastoma-associated protein, Early E1A 32 kDa protein, SULFATE ION, ... (4 entities in total)
• Functional Keywords: retinoblastoma protein, e1a, e2f displacement, transcription repressor, cell cycle
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus : P06400; Host nucleus : P03255
• Total number of polymer chains: 5
• Total formula weight: 85243.78

Authors

Liu, X.,Marmorstein, R. (deposition date: 2007-09-07, release date: 2007-10-02, Last modification date: 2024-02-21)

Primary citation

Liu, X.,Marmorstein, R.
Structure of the retinoblastoma protein bound to adenovirus E1A reveals the molecular basis for viral oncoprotein inactivation of a tumor suppressor
Genes Dev., 21:2711-2716, 2007

PubMed Abstract: The adenovirus (Ad) E1A (Ad-E1A) oncoprotein mediates cell transformation, in part, by displacing E2F transcription factors from the retinoblastoma protein (pRb) tumor suppressor. In this study we determined the crystal structure of the pRb pocket domain in complex with conserved region 1 (CR1) of Ad5-E1A. The structure and accompanying biochemical studies reveal that E1A-CR1 binds at the interface of the A and B cyclin folds of the pRb pocket domain, and that both E1A-CR1 and the E2F transactivation domain use similar conserved nonpolar residues to engage overlapping sites on pRb, implicating a novel molecular mechanism for pRb inactivation by a viral oncoprotein.

PubMed: 17974914
DOI: 10.1101/gad.1590607

Experimental method

X-RAY DIFFRACTION (1.671 Å)