Title : Mutational analysis of the alpha 1a-adrenergic receptor binding pocket of antagonists by radioligand binding assay.

Pub. Date : 2008 Apr

PMID : 18379048






3 Functional Relationships(s)
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1 Previous molecular dynamics studies from our laboratory indicated that the amino acids Asp106 in the third transmembrane domain (TMD), Gln167 in TMD IV of alpha 1a-AR were directly involved in prazosin, tamsulosin and KMD-3213 binding. Prazosin adrenoceptor alpha 1A Homo sapiens
2 On the other hand, the Gln167Phe mutant alpha 1a-AR showed reduced binding affinity for [3H]prazosin. Prazosin adrenoceptor alpha 1A Homo sapiens
3 The results provide direct evidence that these amino acid residues are responsible for the interactions between alpha 1a-AR and radioligand [3H]prazosin as well as tamsulosin and KMD-3213. Prazosin adrenoceptor alpha 1A Homo sapiens