Structural Conservation and E2F Binding Specificity within the Retinoblastoma Pocket Protein Family.

ABSTRACT: The human pocket proteins retinoblastoma (Rb), p107, and p130 are critical negative regulators of the cell cycle and contribute to tumor suppression. While strong structural conservation within the pocket protein family provides for some functional redundancy, important differences have been observed and may underlie the reason that Rb is a uniquely potent tumor suppressor. It has been proposed that distinct pocket protein activities are mediated by their different E2F transcription factor binding partners. In humans, Rb binds E2F1-E2F5, whereas p107 and p130 almost exclusively associate with E2F4 and E2F5. To identify the molecular determinants of this specificity, we compared the crystal structures of Rb and p107 pocket domains and identified several key residues that contribute to E2F s

SUBMITTER: Liban TJ 

PROVIDER: S-EPMC5048593 | biostudies-literature | 2016 Oct

REPOSITORIES: biostudies-literature