Crystal structure of human guanosine monophosphate reductase 2 (GMPR2) in complex with GMP.

@article{Li2006CrystalSO,
  title={Crystal structure of human guanosine monophosphate reductase 2 (GMPR2) in complex with GMP.},
  author={Jixi Li and Zhiyi Wei and Mei Zheng and Xing Gu and Yingfeng Deng and Rui Qiu and Fei Chen and Chaoneng Ji and Weimin Gong and Yi Xie and Y. Mao},
  journal={Journal of molecular biology},
  year={2006},
  volume={355 5},
  pages={
          980-8
        }
}
  • Jixi Li, Zhiyi Wei, +8 authors Y. Mao
  • Published 2 September 2005
  • Chemistry, Medicine
  • Journal of molecular biology
Guanosine monophosphate reductase (GMPR) catalyzes the irreversible and NADPH-dependent reductive deamination of GMP to IMP, and plays a critical role in re-utilization of free intracellular bases and purine nucleosides. Here, we report the first crystal structure of human GMP reductase 2 (hGMPR2) in complex with GMP at 3.0 A resolution. The protein forms a tetramer composed of subunits adopting the ubiquitous (alpha/beta)8 barrel fold. Interestingly, the substrate GMP is bound to hGMPR2… 
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