Chad Sorenson sandbox 1

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Structure of the retinoblastoma protein pocket domain in complex with adenovirus E1A CR1 domain
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Publication Abstract from PubMed
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(as it appears on PubMed at http://www.pubmed.gov), where 17974914 is the PubMed ID number.
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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.
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{{ABSTRACT_PUBMED_17974914}}
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Structure of the retinoblastoma protein bound to adenovirus E1A reveals the molecular basis for viral oncoprotein inactivation of a tumor suppressor., Liu X, Marmorstein R, Genes Dev. 2007 Nov 1;21(21):2711-6. PMID:17974914
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Revision as of 04:15, 22 September 2009

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

Structure of the retinoblastoma protein pocket domain in complex with adenovirus E1A CR1 domain Publication Abstract from PubMed

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.

Structure of the retinoblastoma protein bound to adenovirus E1A reveals the molecular basis for viral oncoprotein inactivation of a tumor suppressor., Liu X, Marmorstein R, Genes Dev. 2007 Nov 1;21(21):2711-6. PMID:17974914

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Chad Sorenson

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