4n8m

From Proteopedia

proteopedia linkproteopedia link

Template:STRUCTURE 4n8m

Contents 1 Structural polymorphism in the N-terminal oligomerization domain of NPM1 2 Function 3 About this Structure 4 Reference

Structural polymorphism in the N-terminal oligomerization domain of NPM1

Template:ABSTRACT PUBMED 24616519

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 with sequence from Lk3 transgenic mice. Full crystallographic information is available from OCA.

Reference

• Mitrea DM, Grace CR, Buljan M, Yun MK, Pytel NJ, Satumba J, Nourse A, Park CG, Madan Babu M, White SW, Kriwacki RW. Structural polymorphism in the N-terminal oligomerization domain of NPM1. Proc Natl Acad Sci U S A. 2014 Mar 25;111(12):4466-71. doi:, 10.1073/pnas.1321007111. Epub 2014 Mar 10. PMID:24616519 doi:http://dx.doi.org/10.1073/pnas.1321007111