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Integrase

crystal structure

HIV integrase is an 31 kd protein produced from the the C-terminal portion of the Pol gene product. The integrase protein contains three domains: an N-terminal HH-CC zinc finger domain believed to be partially responsible for multimerization, a central catalytic domain and an C-terminal DNA binding domain (1). Integrase is responsible for the integration of proviral DNA into the host genome, which is essential for HIV replication. Integrase, therefore, remains a promising potential target for new anti-HIV therapeutics (2).


A ribbon diagram of the catalytic core domain dimer of HIV-1 integrase. The catalytic aspartate and glutamate residues are shown as ball and stick models. (Pers. Comm. F. Dyda, D.R. Davies)



References

  1. ENGELMAN, A; BUSHMAN, F.D.; CRAGIE, R., IDENTIFICATION OF DISCRETE FUNCTIONAL DOMAINS OF HIV-1 INTEGRASE AND THEIR ORGANIZATION WITHIN AN ACTIVE MULTIMERIC COMPLEX.. EMBO J 12:3269-3275 (1993).
  2. ENGLUND, G; THEODORE, T.S.; FREED, E.O., ET AL., INTEGRATION IS REQUIRED FOR PRODUCTIVE INFECTION OF MONOCYTE -DERIVED MACROPHAGES BY HUMAN IMMUNODEFICIENCY VIRUS TYPE I. J VIROL 69:3216 -3219 (1995).




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