|PROSITE documentation PDOC50876 [for PROSITE entry PS50876]|
The retroviral integrase is the enzyme responsible for the insertion of a DNA copy of the viral genome into host DNA, an essential step in the replication cycle of viruses . Integrases comprise three functional and structural domains: the central core domain, which contains the catalytic site, an N-terminal zinc finger and a C-terminal DNA binding domain . The zinc finger has the signature of zinc-binding residues H-x(3)-H-x(23)-C-x(2)-C. The function of this domain is unclear; however, it is required for integration activity and enhances tetramerization in the context of the full-length integrase .
The structure of this domain has been solved , it comprises four helices (see <PDB:1WJA>). The fold is very similar to that of a number of HTH DNA binding motifs, with helices 2 and 3 corresponding to the HTH motif . The third helice is used for dimerization, whereas in the HTH motif it binds DNA.
The profile we developed covers the whole domain.Last update:
April 2004 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Frankel A.D., Young J.A.|
|Title||HIV-1: fifteen proteins and an RNA.|
|Source||Annu. Rev. Biochem. 67:1-25(1998).|
|2||Authors||Esposito D., Craigie R.|
|Title||HIV integrase structure and function.|
|Source||Adv. Virus. Res. 52:319-333(1999).|
|3||Authors||Zheng R., Jenkins T.M., Craigie R.|
|Title||Zinc folds the N-terminal domain of HIV-1 integrase, promotes multimerization, and enhances catalytic activity.|
|Source||Proc. Natl. Acad. Sci. U.S.A. 93:13659-13664(1996).|
|4||Authors||Cai M., Zheng R., Caffrey M., Craigie R., Clore G.M., Gronenborn A.M.|
|Title||Solution structure of the N-terminal zinc binding domain of HIV-1 integrase.|
|Source||Nat. Struct. Biol. 4:567-577(1997).|