| First Author | Schiöth HB | Year | 1998 |
| Journal | Mol Cell Endocrinol | Volume | 139 |
| Issue | 1-2 | Pages | 109-15 |
| PubMed ID | 9705079 | Mgi Jnum | J:48577 |
| Mgi Id | MGI:1270973 | Doi | 10.1016/s0303-7207(98)00067-7 |
| Citation | Schioth HB, et al. (1998) Evidence indicating that the extracellular loops of the mouse MC5 receptor do not participate in ligand binding. Mol Cell Endocrinol 139(1-2):109-15 |
| abstractText | The mMCS receptor was cloned from a genomic library, mutated in the extracellular loops (EL's), expressed and tested for binding to melanocyte stimulating hormone (MSH) peptides. The EL's show low amino acid homology within the MC receptor family. Two mutants of the mMCS receptor were created in order to investigate the participation of these regions in ligand binding. The EL1 and EL3 were separately altered by multiple mutagenesis so that their amino acid sequences became identical with the hMC1 receptor. The mutants were expressed in COS cells and found to bind peptide ligands in the same fashion as the wild type mMCS receptor clone. The results indicate that the amino acids that were mutated in the mMC5 receptor do not participate in binding of MSH peptides. Comparison of the wild type mMCS receptor with the hMC5 receptor showed that it has the same potency order for the MSH peptides but considerably higher affinity than the hMC5 receptor. (C) 1998 Elsevier Science Ireland Ltd. All rights reserved. |
