Nature Communications (Mar 2022)

Structural basis of leukotriene B4 receptor 1 activation

  • Na Wang,
  • Xinheng He,
  • Jing Zhao,
  • Hualiang Jiang,
  • Xi Cheng,
  • Yu Xia,
  • H. Eric Xu,
  • Yuanzheng He

DOI
https://doi.org/10.1038/s41467-022-28820-9
Journal volume & issue
Vol. 13, no. 1
pp. 1 – 10

Abstract

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In the paper, Dr. Wang et al reported a cryo-EM structure of the human leukotriene B4 receptor 1 (BLT1) in complex with its native ligand leukotriene B4 (LTB4) in an active conformation complexed with Gi protein. The structure reveals the molecule determinant of LTB4 binding and the mechanism of receptor activation. These structural information will boost the understanding of LTB4-BLT1 signaling and provide a rational basis for designing novel anti-leukotriene drugs.