Linked Life Data

9240466

Source:http://linkedlifedata.com/resource/pubmed/id/9240466

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1997-8-28
pubmed:abstractText
The human melanocortin 5 receptor (hMC5R) in the melanocortin receptor family has been identified as the receptor with low affinity towards alpha-MSH. Here we show that the glutamine at position 235 and arginine at the position 272 in the hMC5R are contributing to the low affinity of this receptor. Glutamine235 and arginine272 in hMC5R were mutated to lysine (Q235K) and cysteine (R272C), respectively, residues which are conserved at these positions in other melanocortin receptor subtypes. Upon these mutations affinity of alpha-MSH for hMC5R was increased 10-fold for Q235K and 690-fold for R272C mutants, respectively. The results explain the unusually low affinity of the hMC5R to the melanocortic ligands and suggest the importance of these conserved residues in maintaining the high affinity form of melanocortin receptors.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
236
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
489-92
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Glutamine235 and arginine272 in human melanocortin 5 receptor determines its low affinity to MSH.
pubmed:affiliation
Department of Pharmaceutical Bioscience, Biomedical Centre, Uppsala, Sweden.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't