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| [[Image:2qdj.jpg|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_2qdj| PDB=2qdj | SCENE= }} | | {{STRUCTURE_2qdj| PDB=2qdj | SCENE= }} |
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| '''Crystal structure of the Retinoblastoma protein N-domain provides insight into tumor suppression, ligand interaction and holoprotein architecture'''
| | ===Crystal structure of the Retinoblastoma protein N-domain provides insight into tumor suppression, ligand interaction and holoprotein architecture=== |
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| ==Overview==
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| 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. | | The line below this paragraph, {{ABSTRACT_PUBMED_17996702}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17996702 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17996702}} |
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| ==Disease== | | ==Disease== |
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| [[Category: Cyclin fold]] | | [[Category: Cyclin fold]] |
| [[Category: Cyclin wedge]] | | [[Category: Cyclin wedge]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 14:46:37 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:57:41 2008'' |
