Linked Life Data

21090249

Source:http://linkedlifedata.com/resource/pubmed/id/21090249

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2010-11-23
pubmed:abstractText
The regulatory protein S100A2 is localized in the cell nucleus and takes part in the regulation of the cell cycle and cancerogenesis. It belongs to a large family of S100 proteins and can simultaneously bind calcium and zinc ions. Using a direct thermodynamical method of isothermal titration calorimetry we have determined that in the absence of calcium ions the S100A2 protein can bind three zinc ions per each monomer. Besides that it was determined that the thermodynamics of zinc binding to different binding sites on the S100A2 are significantly different. Zinc binding to the first two sites on the S100A2 is enthalpically unfavorable and is driven only by entropic factors, while the binding of the third zinc ion is enthalpically favorable. Analysis of the zinc ion adsorption isotherms shows that their binding occurs in a consecutive order.
pubmed:language
rus
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0026-8984
pubmed:author
pubmed:issnType
Print
pubmed:volume
44
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
938-42
pubmed:dateRevised
2011-3-15
pubmed:meshHeading
pubmed:articleTitle
[Thermodynamics of zinc binding to human S100A2].
pubmed:publicationType
Journal Article, English Abstract, Research Support, Non-U.S. Gov't