Linked Life Data

12069522

Source:http://linkedlifedata.com/resource/pubmed/id/12069522

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2002-6-18
pubmed:abstractText
Previously, the adenovirus proteinase (AVP) had been shown to be stimulated by an 11-amino-acid cofactor pVIc; the crystal structure of an AVP-pVIc complex formed in vitro reveals a disulfide bond between AVP and pVIc. However, that disulfide bond was recently shown not to be required for maximal stimulation of enzyme activity by pVIc in vitro. Is the disulfide bond physiologically relevant or is it an artifact that arose in the crystallization of the complex? Here we show that a disulfide bond between AVP and pVIc is physiologically relevant, because in the virus particle AVP is linked to pVIc via a disulfide bond. This is also the first experimental proof that AVP interacts in vivo with one of its cofactors, all of which were discovered and characterized in vitro. A rationale as to why this apparently unnecessary disulfide bond between AVP and pVIc forms in the virus particle is presented.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0042-6822
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
296
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
234-40
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
In the virion, the 11-amino-acid peptide cofactor pVIc is covalently linked to the adenovirus proteinase.
pubmed:affiliation
Biology Department, Brookhaven National Laboratory, Upton, New York 11973, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.