Linked Life Data

12198302

Source:http://linkedlifedata.com/resource/pubmed/id/12198302

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 9
pubmed:dateCreated
2002-8-28
pubmed:abstractText
Adenovirus proteinase (AVP) is required for the synthesis of infectious virus and is a target for antiviral therapy. The enzyme requires two viral cofactors for activation: pVIc, an 11-amino acid peptide, and the viral DNA. The structure of the enzyme in the absence of cofactors has not been observed. Single crystals of AVP were obtained via microseeding using the hanging-drop vapour-diffusion method with sodium acetate and sodium citrate as precipitants. At the National Synchrotron Light Source at Brookhaven National Laboratory, the native crystal diffracted to a resolution of 0.98 A and an isomorphous heavy-atom derivative diffracted to 1.9 A. Comparison of the structure of AVP with that of the AVP-pVIc complex should reveal the structural basis of activation of the enzyme by pVIc.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0907-4449
pubmed:author
pubmed:issnType
Print
pubmed:volume
58
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1462-4
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Adenovirus proteinase: crystallization and preliminary X-ray diffraction studies to atomic resolution.
pubmed:affiliation
Department of Pharmacological Sciences, State University of New York at Stony Brook, 11794, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't