4N8M: Structural Polymorphism In The N-terminal Oligomerization Domain Of Npm1

Citation:
Abstract
Nucleophosmin (NPM1) is a multifunctional phospho-protein with critical roles in ribosome biogenesis, tumor suppression, and nucleolar stress response. Here we show that the N-terminal oligomerization domain of NPM1 (Npm-N) exhibits structural polymorphism by populating conformational states ranging from a highly ordered, folded pentamer to a highly disordered monomer. The monomer-pentamer equilibrium is modulated by posttranslational modification and protein binding. Phosphorylation drives the equilibrium in favor of monomeric forms, and this effect can be reversed by Npm-N binding to its interaction partners. We have identified a short, arginine-rich linear motif in NPM1 binding partners that mediates Npm-N oligomerization. We propose that the diverse functional repertoire associated with NPM1 is controlled through a regulated unfolding mechanism signaled through posttranslational modifications and intermolecular interactions.
PDB ID: 4N8MDownload
MMDB ID: 118270
PDB Deposition Date: 2013/10/17
Updated in MMDB: 2014/05
Experimental Method:
x-ray diffraction
Resolution: 1.8  Å
Source Organism:
Similar Structures:
Biological Unit for 4N8M: pentameric; determined by author and by software (PISA)
Molecular Components in 4N8M
Label Count Molecule
Proteins (5 molecules)
5
Nucleophosmin(Gene symbol: Npm1)
Molecule annotation
Chemicals (5 molecules)
1
5
* Click molecule labels to explore molecular sequence information.

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