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Crystal structure of the retinoblastoma protein N domain provides insight into tumor suppression, ligand interaction, and holoprotein architecture.

Abstract:

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 ...

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Journal:
Molecular cell
Volume:
28
Issue:
3
Pages:
371-385
Publication date:
2007-11-05
DOI:
EISSN:
1097-4164
ISSN:
1097-2765
URN:
uuid:c0a7bb00-d1a0-4d01-bc9e-9f7e52372a14
Source identifiers:
317746
Local pid:
pubs:317746

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