1n4m
From Proteopedia
(New page: 200px<br /> <applet load="1n4m" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n4m, resolution 2.20Å" /> '''Structure of Rb tum...) |
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| - | [[Image:1n4m.gif|left|200px]]<br /> | + | [[Image:1n4m.gif|left|200px]]<br /><applet load="1n4m" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1n4m" size=" | + | |
caption="1n4m, resolution 2.20Å" /> | caption="1n4m, resolution 2.20Å" /> | ||
'''Structure of Rb tumor suppressor bound to the transactivation domain of E2F-2'''<br /> | '''Structure of Rb tumor suppressor bound to the transactivation domain of E2F-2'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Repression of E2F transcription activity by the retinoblastoma (Rb) tumor | + | Repression of E2F transcription activity by the retinoblastoma (Rb) tumor suppressor through its interaction with the transactivation domain of the E2F transcription factor is one of the central features of G1/S arrest in the mammalian cell cycle. Deregulation of the Rb-E2F interaction results in hyperproliferation, lack of differentiation, and apoptosis, and can lead to cancer. The 2.2-A crystal structure of the Rb pocket complexed with an 18-residue transactivation-domain peptide of E2F-2 reveals that the boomerang-shaped peptide binds to the highly conserved interface between the A-box and the B-box of the Rb pocket in a bipartite manner. The N-terminal segment of the E2F-2 peptide in an extended beta-strand-like structure interacts with helices from the conserved groove at the A-B interface, whereas the C-terminal segment, which contains one 3(10) helix, binds to a groove mainly formed by A-box helices. The flexibility in the middle of the E2F-2 peptide is essential for the tight association of E2F to the Rb pocket. The binding of Rb to the E2F-2 peptide conceals several conserved residues that are crucial for transcription activation of E2F. We provide the structural basis for the Rb-mediated repression of E2F transcription activity without the requirement of histone-modifying enzymes. |
==About this Structure== | ==About this Structure== | ||
| - | 1N4M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1N4M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N4M OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Chang, J | + | [[Category: Chang, J H.]] |
[[Category: Cho, Y.]] | [[Category: Cho, Y.]] | ||
[[Category: Lee, C.]] | [[Category: Lee, C.]] | ||
| - | [[Category: Lee, H | + | [[Category: Lee, H S.]] |
[[Category: protein-peptide complex]] | [[Category: protein-peptide complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:02:12 2008'' |
Revision as of 12:02, 21 February 2008
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Structure of Rb tumor suppressor bound to the transactivation domain of E2F-2
Overview
Repression of E2F transcription activity by the retinoblastoma (Rb) tumor suppressor through its interaction with the transactivation domain of the E2F transcription factor is one of the central features of G1/S arrest in the mammalian cell cycle. Deregulation of the Rb-E2F interaction results in hyperproliferation, lack of differentiation, and apoptosis, and can lead to cancer. The 2.2-A crystal structure of the Rb pocket complexed with an 18-residue transactivation-domain peptide of E2F-2 reveals that the boomerang-shaped peptide binds to the highly conserved interface between the A-box and the B-box of the Rb pocket in a bipartite manner. The N-terminal segment of the E2F-2 peptide in an extended beta-strand-like structure interacts with helices from the conserved groove at the A-B interface, whereas the C-terminal segment, which contains one 3(10) helix, binds to a groove mainly formed by A-box helices. The flexibility in the middle of the E2F-2 peptide is essential for the tight association of E2F to the Rb pocket. The binding of Rb to the E2F-2 peptide conceals several conserved residues that are crucial for transcription activation of E2F. We provide the structural basis for the Rb-mediated repression of E2F transcription activity without the requirement of histone-modifying enzymes.
About this Structure
1N4M is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural basis for the recognition of the E2F transactivation domain by the retinoblastoma tumor suppressor., Lee C, Chang JH, Lee HS, Cho Y, Genes Dev. 2002 Dec 15;16(24):3199-212. PMID:12502741
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