An Automated System for the Analysis of G Protein-Coupled Receptor Transmembrane Binding Pockets: Alignment, Receptor-Based Pharmacophores, and Their Application

@article{Kratochwil2005AnAS,
  title={An Automated System for the Analysis of G Protein-Coupled Receptor Transmembrane Binding Pockets: Alignment, Receptor-Based Pharmacophores, and Their Application},
  author={Nicole A. Kratochwil and Pari Malherbe and Lothar Lindemann and Martin Ebeling and Marius C. Hoener and Andreas M{\"u}hlemann and Richard H. P. Porter and Martin Stahl and Paul R. Gerber},
  journal={Journal of chemical information and modeling},
  year={2005},
  volume={45 5},
  pages={1324-36}
}
G protein-coupled receptors (GPCRs) share a common architecture consisting of seven transmembrane (TM) domains. Various lines of evidence suggest that this fold provides a generic binding pocket within the TM region for hosting agonists, antagonists, and allosteric modulators. Here, a comprehensive and automated method allowing fast analysis and comparison of these putative binding pockets across the entire GPCR family is presented. The method relies on a robust alignment algorithm based on… CONTINUE READING
25 Citations
83 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 25 extracted citations

References

Publications referenced by this paper.
Showing 1-10 of 83 references

Key amino acid residues implicated in the positive allosteric modulation of rat mGlu 5 a receptors by 3 , 3 ′ - difluorobenzaldazine ( DFB )

  • A. Mühlemann, N. A. Ward, N. A. Kratochwil, C. Diener, C. Fischer
  • 2005

Similar Papers

Loading similar papers…