IPR001037
Integrase, C-terminal, retroviral
InterPro entry
Short name | Integrase_C_retrovir |
Overlapping homologous superfamilies |
Description
Integrase comprises three domains capable of folding independently and whose three-dimensional structures are known. However, the manner in which the N-terminal, catalytic core, and C-terminal domains interact in the holoenzyme remains obscure. Numerous studies indicate that the enzyme functions as a multimer, minimally a dimer. The integrase proteins from Human immunodeficiency virus 1 (HIV-1) and Avian sarcoma virus (have been studied most carefully with respect to the structural basis of catalysis. Although the active site of avian virus integrase does not undergo significant conformational changes on binding the required metal cofactor, that of HIV-1 does. This active site-mediated conformational change in HIV-1 reorganises the catalytic core and C-terminal domains and appears to promote an interaction that is favourable for catalysis
[1].
References
Further reading
2. HIV integrase: a target for AIDS therapeutics. Thomas M, Brady L. Trends Biotechnol. 15, 167-72, (1997). View articlePMID: 9161051
3. Substrate recognition by retroviral integrases. Katzman M, Katz RA. Adv. Virus Res. 52, 371-95, (1999). PMID: 10384243
GO terms
Cross References
Representative structure
5llj: Maedi-Visna virus (MVV) integrase C-terminal domain (residues 220-276)