Linked Life Data

2691633

Source:http://linkedlifedata.com/resource/pubmed/id/2691633

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1990-2-22
pubmed:abstractText
Peptides were synthesized based on the cleavage sites in the adenovirus type 2 proteins pVI and pVII. The synthetic peptides were incubated with disrupted, purified adenovirus as a source of proteinase and specific cleavages were monitored by fast protein liquid chromatography and amino acid analysis. Using this approach it was established that all the peptides cleaved were of the form M(L)XGX decreases G or M(L)XGG decreases X. Thus we have shown that the adenoviral proteinase recognizes a specific secondary structure formed by a sequence of at least five amino acids, the main determinants of specificity being two and four residues to the N-terminal side of the bond cleaved. We were able to examine the relevant structural features of the peptide substrates by utilizing the CHEM-X molecular modelling package. Using our consensus sequence we were able to predict the cleavage sites in the viral proteins pVIII, pre-terminal protein (pTP), 11K and IIIa. Octapeptides containing the predicted sites in pVIII and the pTP were synthesized and shown to be cleaved by the proteinase.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0022-1317
pubmed:author
pubmed:issnType
Print
pubmed:volume
70 ( Pt 12)
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3225-34
pubmed:dateRevised
2009-9-29
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Characterization of the adenovirus proteinase: substrate specificity.
pubmed:affiliation
Department of Biochemistry and Microbiology, University of St Andrews, Fife, U.K.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't