PROSITE documentation PDOC50876Zinc finger integrase-type profile
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 [1]. 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 [2]. 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 [3].
The structure of this domain has been solved [3], 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.
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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). | |
| PubMed ID | 9759480 | |
| DOI | 10.1146/annurev.biochem.67.1.1 |
| 2 | Authors | Esposito D. Craigie R. |
| Title | HIV integrase structure and function. | |
| Source | Adv. Virus. Res. 52:319-333(1999). | |
| PubMed ID | 10384240 |
| 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). | |
| PubMed ID | 8942990 |
| 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). | |
| PubMed ID | 9228950 |
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