2qdj
From Proteopedia
(New page: 200px<br /><applet load="2qdj" size="350" color="white" frame="true" align="right" spinBox="true" caption="2qdj, resolution 2.00Å" /> '''Crystal structure of...) |
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==Overview== | ==Overview== | ||
| - | The retinoblastoma susceptibility protein, Rb, has a key role in | + | The retinoblastoma susceptibility protein, Rb, has a key role in regulating cell-cycle progression via interactions involving the central "pocket" and C-terminal regions. While the N-terminal domain of Rb is dispensable for this function, it is nonetheless strongly conserved and harbors missense mutations found in hereditary retinoblastoma, indicating that disruption of its function is oncogenic. The crystal structure of the Rb N-terminal domain (RbN), reveals a globular entity formed by two rigidly connected cyclin-like folds. The similarity of RbN to the A and B boxes of the Rb pocket domain suggests that Rb evolved through domain duplication. Structural and functional analysis provides insight into oncogenicity of mutations in RbN and identifies a unique phosphorylation-regulated site of protein interaction. Additionally, this analysis suggests a coherent conformation for the Rb holoprotein in which RbN and pocket domains directly interact, and which can be modulated through ligand binding and possibly Rb phosphorylation. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Hassler, M.]] | [[Category: Hassler, M.]] | ||
[[Category: Mittnacht, S.]] | [[Category: Mittnacht, S.]] | ||
| - | [[Category: Pearl, L | + | [[Category: Pearl, L H.]] |
[[Category: antitumor protein]] | [[Category: antitumor protein]] | ||
[[Category: cyclin fold]] | [[Category: cyclin fold]] | ||
[[Category: cyclin wedge]] | [[Category: cyclin wedge]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:38:24 2008'' |
Revision as of 16:38, 21 February 2008
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Crystal structure of the Retinoblastoma protein N-domain provides insight into tumor suppression, ligand interaction and holoprotein architecture
Overview
The retinoblastoma susceptibility protein, Rb, has a key role in regulating cell-cycle progression via interactions involving the central "pocket" and C-terminal regions. While the N-terminal domain of Rb is dispensable for this function, it is nonetheless strongly conserved and harbors missense mutations found in hereditary retinoblastoma, indicating that disruption of its function is oncogenic. The crystal structure of the Rb N-terminal domain (RbN), reveals a globular entity formed by two rigidly connected cyclin-like folds. The similarity of RbN to the A and B boxes of the Rb pocket domain suggests that Rb evolved through domain duplication. Structural and functional analysis provides insight into oncogenicity of mutations in RbN and identifies a unique phosphorylation-regulated site of protein interaction. Additionally, this analysis suggests a coherent conformation for the Rb holoprotein in which RbN and pocket domains directly interact, and which can be modulated through ligand binding and possibly Rb phosphorylation.
About this Structure
2QDJ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of the retinoblastoma protein N domain provides insight into tumor suppression, ligand interaction, and holoprotein architecture., Hassler M, Singh S, Yue WW, Luczynski M, Lakbir R, Sanchez-Sanchez F, Bader T, Pearl LH, Mittnacht S, Mol Cell. 2007 Nov 9;28(3):371-85. PMID:17996702
Page seeded by OCA on Thu Feb 21 18:38:24 2008
