Mu Opioid receptor plays an important role in mediating most of diverse
effects of opioids like analgesia, euphoria and dependence. Studies on
Glycosylation Consensus of various receptors showed that it has important roles
in the affinity, desensitization, G-protein coupling and intracellular
signaling. The aim of the present study was to create a mutation in this
consensus of Rat Mu Opioid Receptor (RMOR) for further investigation of its
function. Using nested PCR one mutation was produced, N53Q. The PCR products as
well as the pcDNA3 vector were digested using HindIII and BamHI
restriction enzymes and were ligated and transformed to Ecoli HB101 cells. The
obtained colonies were analyzed for the presence of the inserts using suitable
restriction enzymes. The obtained plasmids are ready for further investigations
in binding assay and function assays like cyclic AMP measurements.
M. Rabbani , H. M. Sadeghi , A. Jafarian-Dehkordi , V. Hajhashemi and A. Rostami , 2005. N53Q Site Directed Mutagenesis of Rat Mu Opioid Receptor and its Cloning Using pcDNA3 Vector. Pakistan Journal of Biological Sciences, 8: 1115-1118.