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Adrenergic receptors. Models for regulation of signal transduction processes.

dc.contributor.author Caron, MG
dc.contributor.author Hnatowich, M
dc.contributor.author Lefkowitz, Robert J
dc.contributor.author Raymond, JR
dc.coverage.spatial United States
dc.date.accessioned 2013-09-24T17:27:49Z
dc.date.issued 1990-02
dc.identifier http://www.ncbi.nlm.nih.gov/pubmed/2105909
dc.identifier.issn 0194-911X
dc.identifier.uri http://hdl.handle.net/10161/7865
dc.description.abstract Adrenergic receptors are prototypic models for the study of the relations between structure and function of G protein-coupled receptors. Each receptor is encoded by a distinct gene. These receptors are integral membrane proteins with several striking structural features. They consist of a single subunit containing seven stretches of 20-28 hydrophobic amino acids that represent potential membrane-spanning alpha-helixes. Many of these receptors share considerable amino acid sequence homology, particularly in the transmembrane domains. All of these macromolecules share other similarities that include one or more potential sites of extracellular N-linked glycosylation near the amino terminus and several potential sites of regulatory phosphorylation that are located intracellularly. By using a variety of techniques, it has been demonstrated that various regions of the receptor molecules are critical for different receptor functions. The seven transmembrane regions of the receptors appear to form a ligand-binding pocket. Cysteine residues in the extracellular domains may stabilize the ligand-binding pocket by participating in disulfide bonds. The cytoplasmic domains contain regions capable of interacting with G proteins and various kinases and are therefore important in such processes as signal transduction, receptor-G protein coupling, receptor sequestration, and down-regulation. Finally, regions of these macromolecules may undergo posttranslational modifications important in the regulation of receptor function. Our understanding of these complex relations is constantly evolving and much work remains to be done. Greater understanding of the basic mechanisms involved in G protein-coupled, receptor-mediated signal transduction may provide leads into the nature of certain pathophysiological states.
dc.language eng
dc.relation.ispartof Hypertension
dc.subject Amino Acid Sequence
dc.subject GTP-Binding Proteins
dc.subject Molecular Sequence Data
dc.subject Receptors, Adrenergic
dc.subject Signal Transduction
dc.subject Structure-Activity Relationship
dc.title Adrenergic receptors. Models for regulation of signal transduction processes.
dc.type Journal article
pubs.author-url http://www.ncbi.nlm.nih.gov/pubmed/2105909
pubs.begin-page 119
pubs.end-page 131
pubs.issue 2
pubs.organisational-group Basic Science Departments
pubs.organisational-group Biochemistry
pubs.organisational-group Cell Biology
pubs.organisational-group Chemistry
pubs.organisational-group Clinical Science Departments
pubs.organisational-group Duke
pubs.organisational-group Duke Cancer Institute
pubs.organisational-group Duke Institute for Brain Sciences
pubs.organisational-group Institutes and Centers
pubs.organisational-group Institutes and Provost's Academic Units
pubs.organisational-group Medicine
pubs.organisational-group Medicine, Cardiology
pubs.organisational-group Neurobiology
pubs.organisational-group Pathology
pubs.organisational-group School of Medicine
pubs.organisational-group Trinity College of Arts & Sciences
pubs.organisational-group University Institutes and Centers
pubs.publication-status Published
pubs.volume 15


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