Residues from transmembrane helices 3 and 5 participate in leukotriene B4 binding to BLT1.

@article{Sabirsh2006ResiduesFT,
  title={Residues from transmembrane helices 3 and 5 participate in leukotriene B4 binding to BLT1.},
  author={Alan Sabirsh and Robert P. Bywater and Jesper Bristulf and Christer Owman and Jesper Z. Haeggstr{\"o}m},
  journal={Biochemistry},
  year={2006},
  volume={45 18},
  pages={5733-44}
}
Leukotrienes are inflammatory mediators that bind to seven transmembrane, G-protein-coupled receptors (GPCRs). Here we examine residues from transmembrane helices 3 and 5 of the leukotriene B4 (LTB4) receptor BLT1 to elucidate how these residues are involved in ligand binding. We have selected these residues on the basis of (1) amino acid sequence analysis, (2) receptor binding and activation studies with a variety of leukotriene-like ligands and recombinant BLT1 receptors, (3) previously… CONTINUE READING
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