Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1997-6-3
pubmed:abstractText
Human immunodeficiency virus type 1 (HIV-1) encodes a trans-acting regulatory protein, termed Rev, which is critically required for virus replication. Rev is a sequence-specific RNA binding protein which mediates the nuclear export of unspliced and incompletely spliced viral mRNAs encoding the viral structural proteins. While CD and fluorescence measurements have provided several possible structural models of Rev, all attempts employing X-ray crystallography and NMR techniques have so far failed to provide more accurate data. We present a new approach to validate alternative structural models of the N-terminal region of Rev which contains the nuclear localization/RNA binding domain. Points of contact between structural elements in a protein were determined by introduction of targeted amino acid substitutions and subsequent scoring of the biological activities. Our data resulted in the suggestion of a new and more refined model of HIV-1 Rev structure which to date has been impossible to obtain by other means.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0269-2139
pubmed:author
pubmed:issnType
Print
pubmed:volume
10
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
103-7
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Probing the structure of the HIV-1 Rev trans-activator protein by functional analysis.
pubmed:affiliation
SANDOZ Research Insitute, Department of Immunodermatology, Vienna, Austria.
pubmed:publicationType
Journal Article