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Identification of ligand binding residues in extracellular loops of the melanocortin 1 receptor.

Abstract：

:To investigate whether residues in the extracellular domains of melanocortin 1 receptor (MC1R) are required for ligand binding, a number of mutants were constructed where charged residues were converted to alanine. The residues targeted for mutagenesis were Ser6, Glu102, Arg109, Asp184, Glu269, and Thr272. The mutant receptor DNAs were transiently expressed in COS-1 cells and their ability to bind [N1e4,D-Phe7]-alpha-MSH (NDP-MSH) was evaluated. Substitution of Asp184 by alanine completely abolished the binding of radiolabelled NDP-MSH as well as ACTH, even though the mutated receptor could be detected on cell surface using anti MC1R specific polyclonal antiserum. Mutations of Ser6, Glu269 and Thr272 resulted in a considerable loss of affinity for radiolabelled NDP-MSH as well as the ability of alpha-MSH to displace the bound radiolabelled NDP-MSH. The results demonstrate that the extracellular loops of human MC1R contain important ligand binding epitopes.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Chhajlani V,Xu X,Blauw J,Sudarshi S

doi

10.1006/bbrc.1996.0266

subject

Has Abstract

pub_date

1996-02-15 00:00:00

pages

521-5

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(96)90266-1

journal_volume

219

pub_type

杂志文章

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