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Solution structure of the HIV-2 TAR-argininamide complex

Academic Article
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Overview

authors

  • Brodsky, A. S.
  • Williamson, James

publication date

  • April 1997

journal

  • Journal of Molecular Biology  Journal

abstract

  • The trans-activating region (TAR) RNA-Tat protein interaction is important for activation of transciption in the human immunodeficiency virus (HIV). A model complex for this interaction composed of the two base bulge HIV-2 TAR and the amide derivative of arginine was studied by multidimensional heteronuclear NMR. Because of the improved spectral properties of the HIV-2 TAR complex, a larger number of NOEs in the bulge region were observed than in earlier studies of the HIV-1 TAR-argininamide complex. A total of 681 NOE distance restraints were collected and used to determine the solution structure of the HIV-2 TAR-argininamide complex. As observed in the previously proposed model from this lab, the two A-form stems co-axially stack and the critical U23 and the argininamide are located in the major groove. Model calculations including non-experimental restraints indicate that U23 is within hydrogen bonding distance to A27 consistent with the formation of a U x A x U base-triple. Base-triple formation helps open the major groove to increase the accessibility of G26 to hydrogen bond donors from the guanidinium group of argininamide. Argininamide binding is stabilized by stacking of the guanidinium group between the bases of A22 and U23, forming an argininamide sandwich.

subject areas

  • Arginine
  • Gene Products, tat
  • HIV-2
  • Humans
  • Magnetic Resonance Spectroscopy
  • Models, Molecular
  • Molecular Sequence Data
  • Nucleic Acid Conformation
  • Protein Binding
  • RNA, Viral
  • Transcriptional Activation
  • tat Gene Products, Human Immunodeficiency Virus
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Research

keywords

  • NMR spectroscopy
  • RNA structure
  • RNA-protein interactions
  • TAR RNA
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Identity

International Standard Serial Number (ISSN)

  • 0022-2836

Digital Object Identifier (DOI)

  • 10.1006/jmbi.1996.0879

PubMed ID

  • 9126842
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Additional Document Info

start page

  • 624

end page

  • 639

volume

  • 267

issue

  • 3

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