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Integrase catalytic domain structure

Schematic domain structure of -I integrase as adapted from Engelman et al. [19]. Structures of two domains, the catalytic core extending from residues 50 to 212 [3] and the nonspecific DNA-binding domain from residues 220 to 270 [28,29], have recently been determined by x-ray crystallography and NMR spectroscopy, respectively. Schematic domain structure of -I integrase as adapted from Engelman et al. [19]. Structures of two domains, the catalytic core extending from residues 50 to 212 [3] and the nonspecific DNA-binding domain from residues 220 to 270 [28,29], have recently been determined by x-ray crystallography and NMR spectroscopy, respectively.
Dyda F, Hickman AB, Jenkins TM, Engelman A, Craigie R, Davies DR. Crystal structure of the catalytic domain of HIV-1 integrase Similarity to other polynucleotidyl transferases. Science 1994 266 1981-1986. [Pg.113]

Members of the structurally related superfamily of enzymes that include RNase H, RuvC resolvase, MuA transposase, and retroviral integrase contain at least three acidic residues in the active site and require divalent cations, such as Mg or Mn ", for their enzymatic activity. However, the precise placement of cations is reported in the X-ray crystal structures of only two of these proteins, E. coli RNase H and HIV-1 RNase H. Details of the location of metal ions in the active site of retroviral integrases can enhance our understanding of the catalytic mechanism of these enzymes and their relationship to that of other members of the superfamily. We present the structure of ASV IN catalytic domain with the essential cations Mg or Mn " " bound in the active site. In addition, we present the structure of an inactive complex of the catalytic domain of ASV IN with Zn ". ... [Pg.417]

Bujacz, G., Jaskolski, M., Alexandratos, J., Wlodawer, A., Merkel, G., Katz, R. A., and Skalka, A. M. (1996). The catalytic domain of avian sarcoma virus integrase conformation of the active-site residues in the presence of divalent cations. Structure 4, 89-96. Kulkosky, J., Katz, R. A., Merkel, G., and Skalka, A. M. (1995). Activities and substrate specificity of the evolutionarily conserved central domain of retroviral integrase. Virology 206, 448-456,... [Pg.424]

IV. Structure Of The Catalytic Core Domain Of HIV-1 Integrase A Description of the Structure... [Pg.91]

The three-dimensional structure of the catalytic core domain of HIV-1 integrase is centered on a mixed five stranded (3 sheet flanked by several helices forming... [Pg.91]

Structures of the catalytic core of HIV-1 integrase, HIV-l RNase H, RuvC, and the core domain of MuA transposase demonstrating similarities in folding topology. The catalytically essential residues... [Pg.95]

Figure 4.5 Example of how crystallographic packing effects can lead to ligand binding modes that are not biologically relevant. The yellow and green structure (PDB ID lqs4 the catalytic core domain of HIV integrase) shows atom coordinates generated by expanding symmetry-related molecules. Figure 4.5 Example of how crystallographic packing effects can lead to ligand binding modes that are not biologically relevant. The yellow and green structure (PDB ID lqs4 the catalytic core domain of HIV integrase) shows atom coordinates generated by expanding symmetry-related molecules.

See other pages where Integrase catalytic domain structure is mentioned: [Pg.83]    [Pg.109]    [Pg.2014]    [Pg.417]    [Pg.424]    [Pg.142]    [Pg.144]    [Pg.248]    [Pg.87]    [Pg.99]    [Pg.112]    [Pg.38]   
See also in sourсe #XX -- [ Pg.418 ]




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