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RESEARCH COMMUNICATION

Structure of the retinoblastoma protein bound to adenovirus E1A reveals the molecular basis for viral oncoprotein inactivation of a tumor suppressor

Program in Gene Expression and Regulation, The Wistar Institute, Philadelphia, Pennsylvania 19104, USA; and Department of Chemistry, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA

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.

[Keywords: Retinoblastoma protein; viral oncoprotein; adenovirus E1A; tumor suppressor; pRb/E1A complex]]

Received July 5, 2007; revised version accepted September 6, 2007.

E-MAIL marmor{at}wistar.org; FAX (215) 898-0381.

Supplemental material is available at http://www.genesdev.org.

Article is online at http://www.genesdev.org/cgi/doi/10.1101/gad.1590607

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