Amin Nader, Nietlispach Daniel, Qamar Seema, Coyle Joe, Chiarparin Elisabetta, Williams Glyn
Astex Pharmaceuticals, 436 Cambridge Science Park, Cambridge, CB4 0QA, UK.
Nuffield Department of Population Health, University of Oxford, Richard Doll Building, Oxford, OX3 7LF, UK.
Biomol NMR Assign. 2016 Oct;10(2):315-20. doi: 10.1007/s12104-016-9691-x. Epub 2016 Jun 29.
Proteins of the NSD family are histone-methyl transferases with critical functions in the regulation of chromatin structure and function. NSD1 and NSD2 are homologous proteins that function as epigenetic regulators of transcription through their abilities to catalyse histone methylation. Misregulation of NSD1 and NSD2 expression or mutations in their genes are linked to a number of human diseases such as Sotos syndrome, and cancers including acute myeloid leukemia, multiple myeloma, and lung cancer. The catalytic domain of both proteins contains a conserved SET domain which is involved in histone methylation. Here we report the backbone resonance assignments and secondary structure information of the catalytic domains of human NSD1 and NSD2.
NSD家族的蛋白质是组蛋白甲基转移酶,在染色质结构和功能的调节中具有关键作用。NSD1和NSD2是同源蛋白质,通过其催化组蛋白甲基化的能力作为转录的表观遗传调节因子。NSD1和NSD2表达的失调或其基因突变与多种人类疾病相关,如索托斯综合征,以及包括急性髓性白血病、多发性骨髓瘤和肺癌在内的癌症。这两种蛋白质的催化结构域都包含一个保守的SET结构域,该结构域参与组蛋白甲基化。在这里,我们报告了人类NSD1和NSD2催化结构域的主链共振归属和二级结构信息。