Tsuda Kengo, Kuwasako Kanako, Nagata Takashi, Takahashi Mari, Kigawa Takanori, Kobayashi Naohiro, Güntert Peter, Shirouzu Mikako, Yokoyama Shigeyuki, Muto Yutaka
RIKEN Systems and Structural Biology Center, Tsurumi-ku, Yokohama, 230-0045, Japan; Division of Structural and Synthetic Biology, RIKEN Center for Life Science Technologies, Tsurumi-ku, Yokohama, 230-0045, Japan.
Proteins. 2014 Oct;82(10):2879-86. doi: 10.1002/prot.24651. Epub 2014 Aug 11.
The family of cytoplasmic polyadenylation element binding proteins CPEB1, CPEB2, CPEB3, and CPEB4 binds to the 3'-untranslated region (3'-UTR) of mRNA, and plays significant roles in mRNA metabolism and translation regulation. They have a common domain organization, involving two consecutive RNA recognition motif (RRM) domains followed by a zinc finger domain in the C-terminal region. We solved the solution structure of the first RRM domain (RRM1) of human CPEB3, which revealed that CPEB3 RRM1 exhibits structural features distinct from those of the canonical RRM domain. Our structural data provide important information about the RNA binding ability of CPEB3 RRM1.
细胞质聚腺苷酸化元件结合蛋白家族CPEB1、CPEB2、CPEB3和CPEB4与mRNA的3'非翻译区（3'-UTR）结合，并在mRNA代谢和翻译调控中发挥重要作用。它们具有共同的结构域组织，包括两个连续的RNA识别基序（RRM）结构域，随后在C端区域有一个锌指结构域。我们解析了人CPEB3第一个RRM结构域（RRM1）的溶液结构，结果表明CPEB3 RRM1具有与典型RRM结构域不同的结构特征。我们的结构数据为CPEB3 RRM1的RNA结合能力提供了重要信息。
