MC4R oligomerizes independently of extracellular cysteine residues.

Abstract:

:The melanocortin 4 receptor (MC4R) plays an essential role in weight regulation. Recently we could show that the MC4R is able to form receptor dimers. In the present study we investigated the role of extracellular cysteine residues and the structure of the third extracellular loop for receptor dimerization. None of the four extracellular cysteine residues nor the structure of the third extracellular loop play a role for MC4R-MC4R interaction as all investigated mutants display the same dimerization pattern as the wild-type receptor. Therefore for MC4R dimerization structures of the transmembrane-spanning helices are more likely to be involved.

journal_name

Peptides

journal_title

Peptides

authors

Elsner A,Tarnow P,Schaefer M,Ambrugger P,Krude H,Grüters A,Biebermann H

doi

10.1016/j.peptides.2005.02.027

subject

Has Abstract

pub_date

2006-02-01 00:00:00

pages

372-9

issue

2

eissn

0196-9781

issn

1873-5169

pii

S0196-9781(05)00449-3

journal_volume

27

pub_type

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