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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    ISSN: 1573-9023
    Keywords: AIDS ; Antiviral agents ; Drug resistance ; Polymerase structure ; Protein-nucleic acid interactions ; Reverse transcriptase inhibitors
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary Two recent X-ray crystallographic studies have resulted in the three-dimensional structure determination of the reverse transcriptase (RT) enzyme from the human immunodeficiency virus type 1 (HIV-1) [Kohlstaedt et al., Science, 256 (1992) 1783; Jacobo-Molina et al., Proc. Natl. Acad. Sci. USA, 90 (1993) 6320]. This report reviews the structure of the reverse transcriptase heterodimer and provides a detailed description of the folding and topology of the individual subdomains. The interactions of the enzyme with bound template- primer are highlighted. Structure-function relationships have been established and are discussed for several conserved sequence motifs located within the enzyme. Each of these motifs is found to interact significantly with template-primer during the polymerization process. This review integrates the findings of both structure determinations, in particular, to relate these structures to strategies for drug design and development. The structures of both the nucleoside and nonnucleoside inhibitor binding sites are described, and the spatial relationship between the two sites is discussed in light of some novel possibilities for drug development. The first indication of an HIV-1 RT drug-resistant mutation manifested in the p51 subunit is presented. This mutation is located in a region of p51 that is proximal to the nonnucleoside binding pocket. The mechanisms of HIV-1 RT inhibition by both nucleoside and nonnucleoside classes of inhibitors are discussed in relation to the structure of the enzyme. In addition, the implications of the structure for understanding and avoiding the development of resistance of HIV-1 reverse transcriptase to antiviral inhibitors are discussed.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature structural & molecular biology 11 (2004), S. 469-474 
    ISSN: 1545-9985
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] Tenofovir, also known as PMPA, R-9-(2-(phosphonomethoxypropyl)adenine, is a nucleotide reverse transcriptase (RT) inhibitor. We have determined the crystal structures of two related complexes of HIV-1 RT with template primer and tenofovir: (i) a ternary complex at a resolution of 3.0 Å of RT ...
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Biopolymers 44 (1997), S. 125-138 
    ISSN: 0006-3525
    Keywords: AIDS ; DNA structure ; polymerase structure ; protein - DNA interaction ; x-ray crystallography ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The conformation of the DNA and the interactions of the nucleic acid with the protein in a complex of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) and a 19-mer/18-mer double-stranded DNA template-primer (dsDNA) are described. The structure of this HIV-1 RT complex with dsDNA serves as a useful paradigm for studying aspects of nucleotide polymerases such as catalysis, fidelity, drug inhibition, and drug resistance. The bound dsDNA has a bend of approximately 41° at the junction of an A-form region (first five base pairs near the polymerase active site) and a B-form region (the last nine base pairs toward the RNase H active site). The 41° bend occurs smoothly over the four base pairs between the A-form portion and the B-form portion in the vicinity of helices αH and αI of the p66 thumb subdomain. The interactions between the dsDNA and protein primarily involve the sugar - phosphate backbone of the nucleic acid and structural elements of the palm, thumb, and RNase H of p66, and are not sequence specific. Amino acid residues from the polymerase active site region, including amino acid residues of the conserved Tyr-Met-Asp-Asp (YMDD) motif and the “primer grip,” interact with 3′-terminal nucleotides of the primer strand and are involved in positioning the primer terminal nucleotide and its 3′-OH group at the polymerase active site. Amino acid residues of the “template grip” have close contacts with the template strand and aid in positioning the template strand near the polymerase active site. Helix αH of the p66 thumb is partly inserted into the minor groove of the dsDNA and helix αI is directly adjacent to the backbone of the template strand. Amino acid residues of Β1′, αA′, αB′, and the loop containing His539 of the RNase H domain interact with the primer strand of the dsDNA. © 1997 John Wiley & Sons, Inc. Biopoly 44: 125-138, 1997
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 357 (1992), S. 85-89 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] **************We have described procedures for the preparation of crystals of a complex of HIV-1 reverse transcriptase, an Fab fragment, and DNA16. The same crystal form can be grown without DNA. We used a 19-base strand paired with an 18-base strand (19/18) dsDNA with a one-base overhang as a ...
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 319 (1986), S. 743-748 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] A biologically active complementary DNA clone of a transforming gene present in a human colon carcinoma contains gene sequences of both tropomyosin and a previously unknown protein tyrosine kinase. The predicted protein (641 amino acids) encoded by this oncogene seems to have been formed by a ...
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  • 6
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 30 (1991), S. 11700-11706 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 30 (1991), S. 11707-11719 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 34 (1995), S. 5351-5363 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Periodontology 2000 2 (1989), S. 0 
    ISSN: 1600-0757
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: A cDNA encoding mouse tyrosinase was inserted into a plasmid containing the provirus of a replication competent avian leukosis virus (ALV). A viral stock produced from the plasmid was used to infect cultured tyrosinase-negative (ca/ca) unpigmented chick embryo melanocytes. Five days after infection many cells were producing very dark discrete melanosomes.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
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