PROSITE documentation PDOC50876
Zinc 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.


Technical section

PROSITE method (with tools and information) covered by this documentation:

ZF_INTEGRASE, PS50876; Zinc finger integrase-type profile  (MATRIX)


1AuthorsFrankel A.D. Young J.A.
TitleHIV-1: fifteen proteins and an RNA.
SourceAnnu. Rev. Biochem. 67:1-25(1998).
PubMed ID9759480

2AuthorsEsposito D. Craigie R.
TitleHIV integrase structure and function.
SourceAdv. Virus. Res. 52:319-333(1999).
PubMed ID10384240

3AuthorsZheng R. Jenkins T.M. Craigie R.
TitleZinc folds the N-terminal domain of HIV-1 integrase, promotes multimerization, and enhances catalytic activity.
SourceProc. Natl. Acad. Sci. U.S.A. 93:13659-13664(1996).
PubMed ID8942990

4AuthorsCai M. Zheng R. Caffrey M. Craigie R. Clore G.M. Gronenborn A.M.
TitleSolution structure of the N-terminal zinc binding domain of HIV-1 integrase.
SourceNat. Struct. Biol. 4:567-577(1997).
PubMed ID9228950

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