Linked Life Data

10795907

Source:http://linkedlifedata.com/resource/pubmed/id/10795907

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2000-6-27
pubmed:abstractText
Although it is now widely accepted that G-protein-coupled receptors exist in at least two allosteric states, inactive and active, and that the spontaneous equilibrium between the two is regulated by various events including the binding of specific agonists and antagonists, the molecular counterparts of these functionally different states are still poorly understood. In this paper, we review our current knowledge concerning the structure-function relationships of the oxytocin and vasopressin receptors, focusing in particular on the process of receptor activation. Using a combined approach of site-directed mutagenesis and molecular modelling, we investigated the molecular events leading to agonist-dependent and -independent receptor activation in the human oxytocin receptor. Our analysis allows us to propose that the active conformations of this receptor are characterised by similar rearrangements of its cytosolic regions that ultimately lead to the opening of a putative docking site for the G-protein. Furthermore, the dynamics of these motions are similar to that observed in the alpha1B-adrenergic receptor, thus suggesting that, although activated by different ligands, the process of receptor isomerization in these two receptors is regulated by the same cluster of highly conserved residues and that common molecular events are responsible for receptor activation in different G-protein-coupled receptors.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0958-0670
pubmed:author
pubmed:issnType
Print
pubmed:volume
85 Spec No
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
59S-66S
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
Molecular basis of ligand binding and receptor activation in the oxytocin and vasopressin receptor family.
pubmed:affiliation
CNR Cellular and Molecular Pharmacology Center, Department of Pharmacology, University of Milan, Italy. b.chini@csfic.mi.cnr.it
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't