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Ligand binding analysis of human neuropeptide Y1 receptor mutants expressed in E. coli

Abstract

Site-directed mutants of the human neuropeptide Y1 (NPY Y1) receptor expressed as a maltose binding protein fusion protein in E. coli show identical ligand binding parameters compared with the same mutants expressed in mammalian cells using a vaccinia virus expression system. However, it was remarkable that two receptor mutants, which were initially classified as non-binding when expressed in an eukaryotic expression system, could actually be revealed to have wild-type binding activity when expressed in E. coli. Re-expression and retesting of these mutants in mammalian cells confirmed this result. This shows that bacterial expression can be used as a fast, versatile and valuable alternative to mammalian expression systems for the analysis of ligand binding sites in G-protein coupled receptors.

Type Journal
ISBN 1060-6823 (Print)
Authors Munch, G.;Walker, P.;Shine, J.;Herzog, H. :
Garvan Authors Prof Herbert Herzog , Prof John Shine
Publisher Name Receptors Channels
Published Date 1995-01-01 00:00:00
Published Volume 3
Published Issue 4
Published Pages 291-7
URL http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8834002
Status Published In-print