3E4U

Crystal Structure of the Wild-Type Human BCL6 BTB/POZ Domain

Summary for 3E4U

• Entry DOI: 10.2210/pdb3e4u/pdb
• Descriptor: B-cell lymphoma 6 protein (2 entities in total)
• Functional Keywords: btb/poz protein interaction domain, activator, dna-binding, metal-binding, nucleus, phosphoprotein, proto-oncogene, repressor, transcription, transcription regulation, zinc-finger
• Biological source: Homo sapiens (Human)
• Cellular location: Nucleus (By similarity): P41182
• Total number of polymer chains: 6
• Total formula weight: 88422.90

Authors

Stead, M.A.,Rosbrook, G.O.,Hadden, J.M.,Trinh, C.H.,Carr, S.B.,Wright, S.C. (deposition date: 2008-08-12, release date: 2008-12-09, Last modification date: 2024-02-21)

Primary citation

Stead, M.A.,Rosbrook, G.O.,Hadden, J.M.,Trinh, C.H.,Carr, S.B.,Wright, S.C.
Structure of the wild-type human BCL6 POZ domain.
Acta Crystallogr.,Sect.F, 64:1101-1104, 2008

PubMed Abstract: BCL6 is a transcriptional repressor that is overexpressed in diffuse large B-cell lymphoma and follicular lymphoma. The N-terminal POZ domain of BCL6 interacts with transcriptional corepressors and targeting these associations is a promising therapeutic strategy. Previous structural studies of the BCL6 POZ domain have used a mutant form because of the low solubility of the wild-type recombinant protein. A method for the purification and crystallization of the wild-type BCL6 POZ domain is described and the crystal structure to 2.1 A resolution is reported. This will be relevant for the design of therapeutics that target BCL6 POZ-domain interaction interfaces.

PubMed: 19052359
DOI: 10.1107/S1744309108036063

Experimental method

X-RAY DIFFRACTION (2.1 Å)