Structural study of MCPIP1 N-terminal conserved domain reveals a PIN-like RNase

@inproceedings{Xu2012StructuralSO,
  title={Structural study of MCPIP1 N-terminal conserved domain reveals a PIN-like RNase},
  author={Jiwei Xu and Wei Peng and Yao Sun and Xiangxi Wang and Yihui Xu and Xuemei Li and Guangxia Gao and Zihe Rao},
  booktitle={Nucleic acids research},
  year={2012}
}
MCP-1-induced protein 1 (MCPIP1) plays an important role in the downregulation of the LPS-induced immune response by acting as an RNase targeting IL-6 and IL-12b mRNAs. A conserved domain located in the N-terminal part of MCPIP1 is thought to be responsible for its RNase activity, but its catalytic mechanism is not well understood due to the lack of an atomic resolution structure. We determined the 3D crystal structure of this MCPIP1 N-terminal conserved RNase domain at a resolution of 2.0… CONTINUE READING