Nam Yunsun, Sliz Piotr, Song Luyan, Aster Jon C, Blacklow Stephen C
Biological and Biomedical Sciences Graduate Program in the Division of Medical Sciences, Harvard Medical School, Boston, MA 02115, USA.
Cell. 2006 Mar 10;124(5):973-83. doi: 10.1016/j.cell.2005.12.037.
Notch receptors transduce essential developmental signals between neighboring cells by forming a complex that leads to transcription of target genes upon activation. We report here the crystal structure of a Notch transcriptional activation complex containing the ankyrin domain of human Notch1 (ANK), the transcription factor CSL on cognate DNA, and a polypeptide from the coactivator Mastermind-like-1 (MAML-1). Together, CSL and ANK create a groove to bind the MAML-1 polypeptide as a kinked, 70 A helix. The composite binding surface likely restricts the recruitment of MAML proteins to promoters on which Notch:CSL complexes have been preassembled, ensuring tight transcriptional control of Notch target genes.
Notch受体通过形成一种复合物在相邻细胞间传递重要的发育信号，该复合物在激活后会导致靶基因转录。我们在此报告一种Notch转录激活复合物的晶体结构，该复合物包含人Notch1的锚蛋白结构域（ANK）、与同源DNA结合的转录因子CSL以及来自共激活因子Mastermind样蛋白1（MAML-1）的一段多肽。CSL和ANK共同形成一个凹槽，以结合呈扭结的70 Å螺旋状的MAML-1多肽。这种复合结合表面可能会限制MAML蛋白募集到已预先组装好Notch:CSL复合物的启动子上，从而确保对Notch靶基因进行严格的转录控制。
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