Linked Life Data

11997175

Source:http://linkedlifedata.com/resource/pubmed/id/11997175

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
2002-5-8
pubmed:databankReference
pubmed:abstractText
The mammalian gonadotropin-releasing hormone receptor (GnRHR), with 327 amino acids, is among the smallest G protein coupled receptors identified. Absent from this receptor is the cytoplasmic tail, characteristic of other members of this superfamily, which frequently mediates desensitization and down-regulation. The fifteen carboxyl terminal residues in the mammalian GnRHR are absolutely conserved, suggesting important roles for these residues. In the current study, mutations of the mammalian GnRHR were made to study the carboxyl terminus. The receptor mutant GnRHR(Ser(326)Ala) was reduced in ligand affinity (117% reduction compared to wild type (wt)), while receptor numbers and internalization remained unchanged. GnRHR(Ser(326)Tyr) was decreased in effector coupling, while ligand affinity remained unchanged compared to wt. These studies also show that, while mutation of Ser(326) caused a change in ligand binding and effector coupling, truncation at this residue (GnRHR[des(326-327)]) had no measurable effect on GnRHR ligand binding, effector coupling or internalization, functions which appear to require different structural determinants than expression and routing. Removal of all three carboxyl terminal residues (Phe(325), Ser(326) and Leu(327)) or mutation of the receptor (GnRHR[Phe(325)Ala]) caused a complete loss of measurable ligand binding and effector coupling, clearly suggesting an unexplained role for Phe(325).
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0303-7207
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
190
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
19-27
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Conserved mammalian gonadotropin-releasing hormone receptor carboxyl terminal amino acids regulate ligand binding, effector coupling and internalization.
pubmed:affiliation
Oregon Regional Primate Research Center and Department of Physiology and Pharmacology, Oregon Health and Science University, 505 NW 185th Avenue, Beaverton, Portland 97006, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't