Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
93
pubmed:dateCreated
1993-3-30
pubmed:abstractText
The structure of the catalytic subunit of cAMP-dependent protein kinase, the first protein kinase structure to be solved, is reviewed. The general architecture of the enzyme is described as well as the active site regions associated with substrate binding and catalysis. In particular, the unique features of the protein kinase nucleotide fold are outlined. While the catalytic subunit is one of the simplest of the protein kinases, it nevertheless serves as a structural framework for the catalytic core of the entire protein kinase family which now includes over 200 important regulatory enzymes. The essential and conserved features of this core are summarized, and a preliminary model of myosin light-chain kinase, based on the structure of the catalytic subunit, is also discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1359-6640
pubmed:author
pubmed:issnType
Print
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
143-52
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
cAMP-dependent protein kinase and the protein kinase family.
pubmed:affiliation
Department of Chemistry, University of California, San Diego, La Jolla 92093-0654.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Review, Research Support, Non-U.S. Gov't