dc.contributor.author |
Raymond, JR |
|
dc.contributor.author |
Hnatowich, M |
|
dc.contributor.author |
Lefkowitz, RJ |
|
dc.contributor.author |
Caron, MG |
|
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 |
https://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.publisher |
Ovid Technologies (Wolters Kluwer Health) |
|
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 |
|
duke.contributor.id |
Lefkowitz, RJ|0096962 |
|
duke.contributor.id |
Caron, MG|0112275 |
|
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 |
|