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- W2014168099 abstract "We solved the structure and traced the complete active site of the catalytic domain of the human immunodeficiency virus type 1 integrase (HIV‐1 IN) with the F185H mutation. The only previously available crystal structure, the F185K mutant of this domain, lacks one of the catalytically important residues, E152, located in a stretch of 12 disordered residues [Dyda et al. (1994) Science 266, 1981–1986]. It is clear, however, that the active site of HIV‐1 IN observed in either structure cannot correspond to that of the functional enzyme, since the cluster of three conserved carboxylic acids does not create a proper metal‐binding site. The conformation of the loop was compared with two different conformations found in the catalytic domain of the related avian sarcoma virus integrase [Bujacz et al. (1995) J. Mol. Biol. 253, 333‐246]. Flexibility of the active site region of integrases may be required in order for the enzyme to assume a functional conformation in the presence of substrate and/or cofactors." @default.
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- W2014168099 date "1996-12-02" @default.
- W2014168099 modified "2023-10-14" @default.
- W2014168099 title "The catalytic domain of human immunodeficiency virus integrase: ordered active site in the F185H mutant" @default.
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- W2014168099 doi "https://doi.org/10.1016/s0014-5793(96)01236-7" @default.
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