PROSITE logo
Black ribbon
We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
Amos Bairoch

PROSITE documentation PDOC50876
Zinc finger integrase-type profile


View entry in original PROSITE document format
View entry in raw text format (no links)
PURL: https://purl.expasy.org/prosite/documentation/PDOC50876

Description

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)


References

1AuthorsFrankel A.D. Young J.A.
TitleHIV-1: fifteen proteins and an RNA.
SourceAnnu. Rev. Biochem. 67:1-25(1998).
PubMed ID9759480
DOI10.1146/annurev.biochem.67.1.1

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



PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.