2qdj | pdb_00002qdj
Crystal structure of the Retinoblastoma protein N-domain provides insight into tumor suppression, ligand interaction and holoprotein architecture
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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 Wed Jan 23 10:52:42 2008
