Linked Life Data

18275836

Source:http://linkedlifedata.com/resource/pubmed/id/18275836

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2008-3-17
pubmed:abstractText
The dimeric interface of severe acute respiratory syndrome coronavirus main protease is a potential target for the anti-SARS drug development. We have generated C-terminal truncated mutants by serial truncations. The quaternary structure of the enzyme was analyzed using both sedimentation velocity and sedimentation equilibrium analytical ultracentrifugation. Global analysis of the combined results showed that truncation of C-terminus from 306 to 300 had no appreciable effect on the quaternary structure, and the enzyme remained catalytically active. However, further deletion of Gln-299 or Arg-298 drastically decreased the enzyme activity to 1-2% of wild type (WT), and the major form was a monomeric one. Detailed analysis of the point mutants of these two amino acid residues and their nearby hydrogen bond partner Ser-123 and Ser-139 revealed a strong correlation between the enzyme activity loss and dimer dissociation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1096-0384
pubmed:author
pubmed:issnType
Electronic
pubmed:day
1
pubmed:volume
472
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
34-42
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Correlation between dissociation and catalysis of SARS-CoV main protease.
pubmed:affiliation
Department of Life Sciences and Institute of Genome Sciences, National Yang-Ming University, 155 Li-Nong Street, Section 2, Taipei 112, Taiwan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't