Summary information and primary citation
- PDB-id
-
3l2r;
DSSR-derived features in text and
JSON formats; DNAproDB
- Class
- recombination-DNA
- Method
- X-ray (2.88 Å)
- Summary
- Crystal structure of the prototype foamy virus (pfv)
intasome in complex with magnesium
- Reference
-
Hare S, Gupta SS, Valkov E, Engelman A, Cherepanov P
(2010): "Retroviral
intasome assembly and inhibition of DNA strand
transfer." Nature, 464,
232-236. doi: 10.1038/nature08784.
- Abstract
- Integrase is an essential retroviral enzyme that binds
both termini of linear viral DNA and inserts them into a
host cell chromosome. The structure of full-length
retroviral integrase, either separately or in complex with
DNA, has been lacking. Furthermore, although clinically
useful inhibitors of HIV integrase have been developed,
their mechanism of action remains speculative. Here we
present a crystal structure of full-length integrase from
the prototype foamy virus in complex with its cognate DNA.
The structure shows the organization of the retroviral
intasome comprising an integrase tetramer tightly
associated with a pair of viral DNA ends. All three
canonical integrase structural domains are involved in
extensive protein-DNA and protein-protein interactions. The
binding of strand-transfer inhibitors displaces the
reactive viral DNA end from the active site, disarming the
viral nucleoprotein complex. Our findings define the
structural basis of retroviral DNA integration, and will
allow modelling of the HIV-1 intasome to aid in the
development of antiretroviral drugs.
