Linked Life Data

6712933

Source:http://linkedlifedata.com/resource/pubmed/id/6712933

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1984-6-7
pubmed:abstractText
Blue Dextran has been shown to interact specifically with the nucleotide binding site of the catalytic subunit of cAMP-dependent protein kinase. By observing changes in the induced dichroism associated with the absorbance of the bound chromophore, one can monitor conformational changes in the immediate vicinity of the ATP binding site. With this technique, it has been possible to demonstrate that attachment of ligand at the protein substrate binding site of the enzyme results in a conformational change at the ATP binding site. This alteration takes place in at least two steps, one of which appears to be dependent on the presence of a phosphorylatable hydroxyl group on the substrate and the other being triggered by the "basic subsite" (usually one or more arginine residues) to the N-terminal side of the target serine or threonine. Competition experiments suggest that the change induced results in closure over the substrate protein after the initial electrostatic binding; the movement initiated by the presence of a serine hydroxyl group may also involve interaction with a tyrosine residue at the surface of the ATP binding site.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
28
pubmed:volume
23
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
968-73
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Ligand binding site interaction in adenosine cyclic 3',5'-monophosphate dependent protein kinase catalytic subunit: circular dichroic evidence for intramolecular transmission of conformational change.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't