1R28

Crystal Structure of the B-Cell Lymphoma 6 (BCL6) BTB domain to 2.2 Angstrom

Summary for 1R28

• Entry DOI: 10.2210/pdb1r28/pdb
• Related: 1R29 1R2B
• Descriptor: B-cell lymphoma 6 protein (2 entities in total)
• Functional Keywords: btb domain, b-cell lymphoma, transcriptional repression, transcription
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus (By similarity): P41182
• Total number of polymer chains: 2
• Total formula weight: 29119.65

Authors

Ahmad, K.F.,Melnick, A.,Lax, S.A.,Bouchard, D.,Liu, J.,Kiang, C.L.,Mayer, S.,Licht, J.D.,Prive, G.G. (deposition date: 2003-09-26, release date: 2003-12-23, Last modification date: 2024-02-14)

Primary citation

Ahmad, K.F.,Melnick, A.,Lax, S.,Bouchard, D.,Liu, J.,Kiang, C.L.,Mayer, S.,Takahashi, S.,Licht, J.D.,Prive, G.G.
Mechanism of SMRT corepressor recruitment by the BCL6 BTB domain.
Mol.Cell, 12:1551-1564, 2003

PubMed Abstract: BCL6 encodes a transcription factor that represses genes necessary for the terminal differentiation of lymphocytes within germinal centers, and the misregulated expression of this factor is strongly implicated in several types of B cell lymphoma. The homodimeric BTB domain of BCL6 (also known as the POZ domain) is required for the repression activity of the protein and interacts directly with the SMRT and N-CoR corepressors that are found within large multiprotein histone deacetylase-containing complexes. We have identified a 17 residue fragment from SMRT that binds to the BCL6 BTB domain, and determined the crystal structure of the complex to 2.2 A. Two SMRT fragments bind symmetrically to the BCL6 BTB homodimer and, in combination with biochemical and in vivo data, the structure provides insight into the basis of transcriptional repression by this critical B cell lymphoma protein.

PubMed: 14690607
DOI: 10.1016/S1097-2765(03)00454-4

Experimental method

X-RAY DIFFRACTION (2.2 Å)