Ligand binding pocket of the human somatostatin receptor 5: mutational analysis of the extracellular domains.

@article{Greenwood1997LigandBP,
  title={Ligand binding pocket of the human somatostatin receptor 5: mutational analysis of the extracellular domains.},
  author={Michael T Greenwood and N Hukovi{\'c} and Ujendra Kumar and Rosemarie Panetta and Siv A. Hjorth and Coimbatore B. Srikant and Yogesh C. Patel},
  journal={Molecular pharmacology},
  year={1997},
  volume={52 5},
  pages={807-14}
}
The ligand binding domain of G protein-coupled receptors for peptide ligands consists of a pocket formed by extracellular and transmembrane domain (TM) residues. In the case of somatostatin (SRIF), however, previous studies have suggested that the binding cavity of the octapeptide analog SMS201-995 (SMS) is lined by residues in TMs III-VII. The additional involvement of the extracellular domains for binding SMS or the natural SRIF ligands (SRIF-14, SRIF-28) has not been clarified. Using a… CONTINUE READING