Crystal structure of the catalytic domain of HIV-1 integrase: similarity to other polynucleotidyl transferases.

作者: F Dyda , A. Hickman , T. Jenkins , A Engelman , R Craigie

DOI: 10.1126/SCIENCE.7801124

关键词:

摘要: HIV integrase is the enzyme responsible for inserting viral DNA into host chromosome; it essential replication. The crystal structure of catalytically active core domain (residues 50 to 212) HIV-1 was determined at 2.5 A resolution. central feature a five-stranded beta sheet flanked by helical regions. overall topology reveals that this belongs superfamily polynucleotidyl transferases includes ribonuclease H and Holliday junction resolvase RuvC. site region identified position two conserved carboxylate residues catalysis, which are located similar positions in H. In crystal, molecules form dimer with extensive solvent-inaccessible interface 1300 A2 per monomer.

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