Structural rearrangements on HIV-1 Tat (32-72) TAR complex formation
| Autor: | Clemens Steegborn, Andrea Volkmann, Paul Rösch, Margot Kraft, Armin U. Metzger, Dieter Willbold, Rainer Frank, Thomas Schindler |
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| Rok vydání: | 1996 |
| Předmět: |
Models
Molecular Circular dichroism Protein Conformation Ultraviolet Rays UV melting viruses Molecular Sequence Data Biophysics Human immunodeficiency virus (HIV) Nerve Tissue Proteins medicine.disease_cause Hiv 1 tat complex mixtures Biochemistry Genome Tar (tobacco residue) Structural Biology Spectroscopy Fourier Transform Infrared Genetics medicine Tat-TAR interaction Amino Acid Sequence RNA Messenger Molecular Biology Gene biology Chemistry RNA-Binding Proteins Fourier transform infrared spectroscopy RNA Bovine immunodeficiency virus Cell Biology biology.organism_classification Cell biology DNA-Binding Proteins Gene Products tat HIV-1 RNA Viral tat Gene Products Human Immunodeficiency Virus (HIV-1) |
| Zdroj: | FEBS Letters. 384:255-259 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/0014-5793(96)00314-6 |
| Popis: | Expression of the early genes of the human immunodeficiency virus type-1 (HIV-1) genome is under the control of a trans-activator (Tat) protein. HIV-1 Tat action requires binding to TAR (trans-activation responsive element), an RNA sequence located at the 5′-end of all lentiviral mRNAs. We used various spectroscopic methods to investigate conformational changes on HIV-1 TAR binding to the HIV-1 (32–72) Tat peptide BP1. It comprises the RNA binding region and binds specifically to TAR. We conclude from our experiments that the regular A-form of the TAR RNA is slightly distorted towards the B-form when bound to BP1. Thus, the major groove is widened and the binding of BP1 facilitated. BP1 presumably adopts an extended conformation when binding to TAR and may fit well into the TAR major groove. |
| Databáze: | OpenAIRE |
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