Source:http://linkedlifedata.com/resource/pubmed/id/17433255
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
|
pubmed:dateCreated |
2007-4-25
|
pubmed:abstractText |
Aurora-A is a centrosome-localized serine/threonine kinase that is overexpressed in multiple human cancers. Here, we report an intramolecular inhibitory regulation in Aurora-A between its N-terminal regulatory domain (aa 1-128, Nt) and the C-terminal catalytic domain (aa 129-403, Cd). Removal of Nt results in a significant increase in kinase activity. Nt inhibited the activity of the single C-terminal kinase domain, but had little effect on the activity of the full-length of Aurora-A. PP1 is not involved in this regulation, instead, Nt interacts Cd directly in vitro and in vivo. The non-Aurora box (aa 64-128) in the N-terminal negatively regulated the kinase activity of the C-terminal kinase domain by intramolecular interaction with aa 240-300 within the C-terminal.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Jun
|
pubmed:issn |
0006-291X
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
1
|
pubmed:volume |
357
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
347-52
|
pubmed:dateRevised |
2011-7-11
|
pubmed:meshHeading |
pubmed-meshheading:17433255-Binding Sites,
pubmed-meshheading:17433255-Cell Line,
pubmed-meshheading:17433255-Enzyme Activation,
pubmed-meshheading:17433255-Enzyme Inhibitors,
pubmed-meshheading:17433255-Humans,
pubmed-meshheading:17433255-Kidney,
pubmed-meshheading:17433255-Protein Binding,
pubmed-meshheading:17433255-Protein Structure, Tertiary,
pubmed-meshheading:17433255-Protein-Serine-Threonine Kinases,
pubmed-meshheading:17433255-Structure-Activity Relationship
|
pubmed:year |
2007
|
pubmed:articleTitle |
Identification of the auto-inhibitory domains of Aurora-A kinase.
|
pubmed:affiliation |
State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Sciences, Fudan University, Shanghai 200433, China.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|