Backbone resonance assignment of the BCL6-BTB/POZ domain.

BCL6 is a transcriptional repressor. Two domains of the protein, the N-terminal BTB-POZ domain and the RD2 domain are responsible for recruitment of co-repressor molecules and histone deacetylases. The BTB-POZ domain is found in a large and diverse range of proteins that play important roles in development, homeostasis and neoplasia. Crystal structures of several BTB-POZ domains, including BCL6 have been determined. The BTB-POZ domain of BCL6 not only mediates dimerisation but is also responsible for recruitment of co-repressors such as SMRT, NCOR and BCOR. Interestingly both SMRT and BCOR bind to the same site within the BCL6 BTB-POZ domain despite having very different primary sequences. Since both peptides and small molecules have been shown to bind to the co-repressor binding site it would suggest that the BTB_POZ domain is a suitable target for drug discovery. Here we report near complete backbone 15N, 13C and 1H assignments for the BTB-POZ domain of BCL6 to assist in the analysis of binding modes for small molecules.

BCL6是一种转录抑制因子。该蛋白的两个结构域，即N端的BTB - POZ结构域和RD2结构域负责招募共抑制分子和组蛋白去乙酰化酶。BTB - POZ结构域存在于大量不同的蛋白质中，这些蛋白质在发育、体内平衡和肿瘤形成中发挥重要作用。包括BCL6在内的几种BTB - POZ结构域的晶体结构已经确定。BCL6的BTB - POZ结构域不仅介导二聚化，还负责招募诸如SMRT、NCOR和BCOR等共抑制因子。有趣的是，尽管SMRT和BCOR的一级序列差异很大，但它们都结合在BCL6的BTB - POZ结构域内的同一位置。由于肽段和小分子都已被证明能结合到共抑制因子结合位点，这表明BTB - POZ结构域是药物研发的一个合适靶点。在此我们报道了BCL6的BTB - POZ结构域近乎完整的主链15N、13C和1H的归属，以协助分析小分子的结合模式。