2NA1
ULD complex
Summary for 2NA1
| Entry DOI | 10.2210/pdb2na1/pdb |
| NMR Information | BMRB: 25923 |
| Descriptor | Polycomb complex protein BMI-1, Polyhomeotic-like 2 (1 entity in total) |
| Functional Keywords | bmi1, phc2, transcription |
| Biological source | mouse, Homo sapiens (Mus musculus, human) |
| Cellular location | Nucleus : P35226 |
| Total number of polymer chains | 1 |
| Total formula weight | 18229.28 |
| Authors | Cierpicki, T.,Gray, F.,Cho, H. (deposition date: 2015-12-17, release date: 2016-11-16, Last modification date: 2024-05-15) |
| Primary citation | Gray, F.,Cho, H.J.,Shukla, S.,He, S.,Harris, A.,Boytsov, B.,Jaremko, M.,Jaremko, M.,Demeler, B.,Lawlor, E.R.,Grembecka, J.,Cierpicki, T. BMI1 regulates PRC1 architecture and activity through homo- and hetero-oligomerization. Nat Commun, 7:13343-13343, 2016 Cited by PubMed Abstract: BMI1 is a core component of the polycomb repressive complex 1 (PRC1) and emerging data support a role of BMI1 in cancer. The central domain of BMI1 is involved in protein-protein interactions and is essential for its oncogenic activity. Here, we present the structure of BMI1 bound to the polyhomeotic protein PHC2 illustrating that the central domain of BMI1 adopts an ubiquitin-like (UBL) fold and binds PHC2 in a β-hairpin conformation. Unexpectedly, we find that the UBL domain is involved in homo-oligomerization of BMI1. We demonstrate that both the interaction of BMI1 with polyhomeotic proteins and homo-oligomerization via UBL domain are necessary for H2A ubiquitination activity of PRC1 and for clonogenic potential of U2OS cells. Here, we also emphasize need for joint application of NMR spectroscopy and X-ray crystallography to determine the overall structure of the BMI1-PHC2 complex. PubMed: 27827373DOI: 10.1038/ncomms13343 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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