Probing the structure of the HIV-1 Rev trans-activator protein by functional analysis
| Autor: | S L Thomas, J Hauber, Georg Casari |
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| Rok vydání: | 1997 |
| Předmět: |
Models
Molecular Protein Conformation viruses Bioengineering RNA-binding protein Computational biology Protein Engineering Biochemistry Animals Humans Nuclear export signal Molecular Biology chemistry.chemical_classification Regulation of gene expression Binding Sites Molecular Structure Chemistry RNA rev Gene Products Human Immunodeficiency Virus Amino acid Gene Products rev Phenotype Viral replication COS Cells HIV-1 Mutagenesis Site-Directed Nuclear localization sequence Biotechnology Binding domain |
| Zdroj: | Protein Engineering Design and Selection. 10:103-107 |
| ISSN: | 1741-0134 1741-0126 |
| DOI: | 10.1093/protein/10.2.103 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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