Cysteine residues are involved in structure and function of melanocortin 1 receptor: Substitution of a cysteine residue in transmembrane segment two converts an agonist to antagonist.

doi:10.1006/bbrc.2001.4429

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Article

Cysteine residues are involved in structure and function of melanocortin 1 receptor: Substitution of a cysteine residue in transmembrane segment two converts an agonist to antagonist.

Biochemical and biophysical research communications - 9 Mar 2001

Frändberg P A, Doufexis M, Kapas S, Chhajlani V

Abstract excerpt

Reduction of disulfide bonds in human melanocortin 1 receptor (hMC1R) with increasing concentrations of DTT (dithiothreitol) resulted in a decrease in the binding of [125I]-ACTH (adrenocorticotropic hormone, L-isomer) in an uniphasic manner and a decrease in [125I]-NDP-MSH ([Nle(4),D-Phe(7)]-alpha-melanocyte stimulating hormone; D-isomer) binding in a biphasic manner. Pretreatment of hMC1R with 10 mM DTT resulted...

Topics

Adrenocorticotropic Hormone
Amino Acid Sequence
Amino Acid Substitution
Animals
Binding, Competitive
COS Cells
Cyclic AMP
Cysteine
DNA, Recombinant
Dithiothreitol

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Dose-Response Relationship, Drug

Humans

Iodine Radioisotopes

Membrane Proteins

Molecular Sequence Data

Mutagenesis, Site-Directed

Mutation

Radioligand Assay

Source

Open in PubMed

Identifiers

PMID: 11237737
DOI: 10.1006/bbrc.2001.4429

Genes

Variants

Provenance

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