Binding site analysis of full-length alpha1a adrenergic receptor using homology modeling and molecular docking

Biochem Biophys Res Commun. 2004 Jun 25;319(2):493-500. doi: 10.1016/j.bbrc.2004.04.149.


The recent availability of crystal structure of bovine rhodopsin offers new opportunities in order to approach the construction of G protein coupled receptors. This study focuses the attention on the modeling of full-length alpha(1a) adrenergic receptor (alpha(1a)-AR) due to its biological role and significant implications in pharmacological treatment of benign prostate hyperplasia. This work could be considered made up by two main steps: (a) the construction of full structure of alpha(1a)-AR, through homology modeling methods; (b) the automated docking of an endogenous agonist, norepinephrine, and of an antagonist, WB-4101, using BioDock program. The obtained results highlight the key residues involved in binding sites of both agonists and antagonists, confirming the mutagenesis data and giving new suggestions for the rational design of selective ligands.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Cattle
  • Models, Molecular
  • Molecular Sequence Data
  • Norepinephrine / metabolism
  • Protein Conformation
  • Receptors, Adrenergic, alpha-1 / chemistry
  • Receptors, Adrenergic, alpha-1 / genetics
  • Receptors, Adrenergic, alpha-1 / metabolism*
  • Sequence Homology, Amino Acid


  • Receptors, Adrenergic, alpha-1
  • Norepinephrine