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
Peptidesjournal_title
Peptidesauthors
Elsner A,Tarnow P,Schaefer M,Ambrugger P,Krude H,Grüters A,Biebermann Hdoi
10.1016/j.peptides.2005.02.027subject
Has Abstractpub_date
2006-02-01 00:00:00pages
372-9issue
2eissn
0196-9781issn
1873-5169pii
S0196-9781(05)00449-3journal_volume
27pub_type
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