Linked Life Data

6128188

Source:http://linkedlifedata.com/resource/pubmed/id/6128188

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
90
pubmed:dateCreated
1983-1-7
pubmed:abstractText
Hormone-sensitive adenylate cyclase systems are composed of hormone-recognition units (R), a nucleotide-regulatory unit (N) for reaction with GTP and divalent cations, and the catalytic unit (C). From the reported sizes of purified R and N subunits and target analysis of functional sizes of these units, the functions of the components for the binding and actions of hormones and GTP require minimally dimers, homologous or heterologous. It is proposed that the catalytic unit exists in the membrane also as a dimer and that its transition to the active state with MgATP as substrate involves corresponding transitions in linked dimers of the hormone-recognition and nucleotide-regulatory units. It is postulated that hormones trigger the activation process by inducing in concert with GTP and divalent cations the appropriate dimer structure of the holoenzyme. In large aggregates of such structures, realignment of only a few occupied holoenzyme units may be sufficient to induce activation of the total aggregate enzyme. This theory serves to explain the synergistic actions of hormones, and how several hormones can activate a common enzyme. It also provides an explanation for 'spare' receptors, and for the efficacy of hormone action.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0300-5208
pubmed:author
pubmed:issnType
Print
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3-21
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Structure-function relationships in adenylate cyclase systems.
pubmed:publicationType
Journal Article