Linked Life Data

12482133

Source:http://linkedlifedata.com/resource/pubmed/id/12482133

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2002-12-16
pubmed:abstractText
The protein kinase C (PKC)-mediated phosphorylation of the Na(+)/K(+)-ATPase alpha-subunit has been shown to play an important role in regulation of the Na(+)/K(+)-ATPase activity. In the rat alpha1-subunit, phosphorylation occurs at Ser-23 and results in inhibition of the transport function of the Na(+)/K(+)-ATPase, which is mimicked by replacing the Ser-23 by the negatively charged glutamic acid or by aspartic acid. Using comparative molecular modeling, we investigated whether phosphorylation or acidic replacement at position 23 causes a dramatic change in the molecular electrostatic potential at position 23 as a result of insertion of a negative charge of the phosphoryl group or Glu per se, or whether, alternatively, the modification causes larger-scale conformational changes in the N-terminus of the alpha-subunit. The results predict a considerable conformational change of the 30-residue stretch around Ser-23 when mutated to the residues carrying a net negative charge or being phosphorylated. The structural rearrangements occur within the N-terminal helix-loop-helix motif with a set of charged residues. This motif has structural homology with one in the Ca(2+)-ATPase and may form a function-related structural site in the P-type ATPases. Comparative molecular modeling indicates a lengthening of the interhelical loop and an order-to-disorder transition by disrupting a helix at position 23 because of posphorylation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1085-9195
pubmed:author
pubmed:issnType
Print
pubmed:volume
37
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
83-95
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Predicted alterations in tertiary structure of the N-terminus of Na(+)/K(+)-ATPase alpha-subunit caused by phosphorylation or acidic replacement of the PKC phosphorylation site Ser-23.
pubmed:affiliation
Leibniz-Institute for Plant Biochemistry, Weinberg 3, D-06120 Halle/Salle, Germany.
pubmed:publicationType
Journal Article, Comparative Study, In Vitro, Research Support, Non-U.S. Gov't