Skip to main content
. Author manuscript; available in PMC: 2009 Jun 24.
Published in final edited form as: Biochem Pharmacol. 2008 Sep 30;77(1):114–124. doi: 10.1016/j.bcp.2008.09.023

Table 3.

Mutations of the non-conserved residues in TM6 of the hMC4R on DNaI(2′)8-γ-MSH binding and CAMP production. All determinations were on cells transfected with wild type or mutated receptors. Ki values for [Pro5, DNaI(2′)8]-γ-MSH were determined from displacement of 125I-NDP-MSH binding, as described under “Section 2”. The data shown are mean ± S.E.M of at least three independant experiments.

Receptor expression [Pro5, DNaI(2′)8]-γ-MSH
Ki (nM) EC50(nM) Emax(%)
hMC1RWT 100 2.1±0.1 0.3±0.02 100
I266T 95±15.4 133.3±18.2 Partial agonist 33
F267L 96±12.2 169.3±21.2 Partial agonist 32
Y268I 94±3.5 154.2±11.1 Partial agonist 45
I269V 92±7.7 212.9±30.3 Partial agonist 51
S270L 93±8.1 124.3±12.5 Partial agonist 30
hMC4-WT 100 126.6±13.1 Partial agonist 35