Characterisation of D117A and H260A mutations in the melanocortin 1 receptor

Helgi B. Schiöth, Ruta Muceniece, Michael Szardenings, Peteris Prusis, Gunnar Lindeberg, Shubh D. Sharma, Victor J. Hruby, Jarl E.S. Wikberg

Research output: Contribution to journalArticlepeer-review

22 Scopus citations

Abstract

Recent site directed mutagenesis studies on the melanocortin 1 (MC1) receptor have indicated the importance of D117 and H260 amino acid residues for the binding of α-MSH (melanocyte stimulating hormone). Here, we report the testing of 12 cyclic and linear MSH peptides on the D117A and H260A mutant receptors. Moreover, we constructed a double mutant which displayed a major loss in affinity for [Nle4, D-Phe7]α-MSH. Our new data of His6 and Phe7 substituted MSH peptides are compared with previous results and the hypothesis of putative interactions of D117 and H260 with single amino acids in the MSH peptide. Our conclusions are that the D117A and the H260A mutations may cause conformational changes in the receptor which can not be linked to any specific amino acid in the MSH-peptides.

Original languageEnglish (US)
Pages (from-to)213-219
Number of pages7
JournalMolecular and Cellular Endocrinology
Volume126
Issue number2
DOIs
StatePublished - Feb 7 1997

Keywords

  • Ligand binding
  • MC1 receptor
  • MSH
  • Mutagenesis

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Endocrinology

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