Protein Engineering, Vol 10, 103-107, Copyright © 1997 by Oxford University Press
SL Thomas, J Hauber and G Casari
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.
ARTICLES
Probing the structure of the HIV-1 Rev trans-activator protein by functional analysis
SANDOZ Research Insitute, Department of Immunodermatology, Vienna, Austria.
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