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Comment
. 2003 Mar 4;100(5):2165-7.
doi: 10.1073/pnas.0630419100. Epub 2003 Feb 26.

Clefts, grooves, and (small) pockets: the structure of the retinoblastoma tumor suppressor in complex with its cellular target E2F unveiled

Karl Munger  1
Affiliations
Comment

Clefts, grooves, and (small) pockets: the structure of the retinoblastoma tumor suppressor in complex with its cellular target E2F unveiled

Karl Munger. Proc Natl Acad Sci U S A. .
No abstract available

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Figures

Figure 1
Figure 1
The retinoblastoma tumor suppressor pathway contains multiple oncogenes (green) and tumor suppressors (red) and is dysfunctional in almost every human tumor. Even though E2F is an important mediator of the growth suppressor function of pRb, no activating E2F mutants have been detected in human tumors.
Figure 2
Figure 2
Schematic representation of the pRb, E2F, and E7 domains discussed here. E2F interacts through a linear sequence within the activation domain (AD) shown in green with a cleft formed by three non- contiguous regions within domains A and B of the pRb pocket (green). The HPV E7 protein interacts with the LXCXE domain (yellow) with a groove formed by two noncontiguous sequences within domain B of the pocket. The two interaction domains are ≈30 Å apart and on different faces of the pocket. The marked box (M) in E2F and the amino (N)- and carboxyl (C)-terminal domains as well as the flexible spacer (S) between domains A and B of the pRb pocket are also indicated. Areas of pRb, E2F, and E7 shown in gray represent structural terra incognita. See text for details.
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