Abstract:
One-third of eukaryotic proteins are associated with
membranes and these membrane proteins (MP) represent approximately
50% of pharmacological targets. Researchers are therefore nursing the
hope of achieving a higher percentage of about 80% in the near future.
The only bottleneck to achieving this target is the experimental
challengers associated with the production, purification and
crystallization at reasonable cost. Expression of protein in E. coli is now
very popular, because it is easy to use and also comes with low
operational cost. But membrane proteins have been difficult to produce
in E. coli. The membrane proteins (MP), G-protein coupled receptors
(GPCRs) represent the major class of potential drug targets but probably
the most difficult class of MPs to bring to three-dimensional studies.
This review paper therefore sought to bring to the fore some of the
techniques employed by researchers to improve the quality and quantity
of GPCR expressed in E. coli. A literature search on the effective
expression of some important members of the GPCR family in E. coli
was done. The Expression of neurotensin receptor type1 (NTIS1) in
BL21 (DE3) and C41 (DE3) strains of E. coli; Autoinduction of NTS1 in
BL21 (DE3) with the medium Magicmedia™; Expression in E. coli by
targeting the inner membrane with fusion partners MBP and TRX
(MBP-GPCR-TRX); Expression in E. coli by targeting the inclusion
bodies with fusion partners GST and TRX; and the use of pDEST17
vectors and C43 strain at 37oC have proved experimentally efficient to
express highly functional GPCR
