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4n8m
From Proteopedia
Structural polymorphism in the N-terminal oligomerization domain of NPM1
Function
[NPM_MOUSE] Involved in diverse cellular processes such as ribosome biogenesis, centrosome duplication, protein chaperoning, histone assembly, cell proliferation, and regulation of tumor suppressors p53/TP53 and ARF. Binds ribosome presumably to drive ribosome nuclear export. Acts as a chaperonin for the core histones H3, H2B and H4. Stimulates APEX1 endonuclease activity on apurinic/apyrimidinic (AP) double-stranded DNA but inhibits APEX1 endonuclease activity on AP single-stranded RNA. May exert a control of APEX1 endonuclease activity within nucleoli devoted to repair AP on rDNA and the removal of oxidized rRNA molecules (By similarity). Associated with nucleolar ribonucleoprotein structures and bind single-stranded nucleic acids. In concert with BRCA2, regulates centrosome duplication. Regulates centriole duplication: phosphorylation by PLK2 is able to trigger centriole replication (By similarity). Negatively regulates the activation of EIF2AK2/PKR and suppresses apoptosis through inhibition of EIF2AK2/PKR autophosphorylation (By similarity).
About this Structure
4n8m is a 5 chain structure. Full crystallographic information is available from OCA.
Categories: Babu, M M. | Buljan, M. | Kriwacki, R W. | Mitrea, D. | Nourse, A. | Park, C. | Pytel, N. | Royappa, G. | Satumba, J. | White, S W. | Yun, M. | Chaperone | Histone chaperone | Nucleolar protein | Pentamer | Phosphoprotein | Regulated unfolding | Ribosome biogenesis | Structural polymorphism
