Crystal structure of the HIV-1 integrase core domain in complex with sucrose reveals details of an allosteric inhibitory binding site

Journal Article · Mon Apr 19 04:00:00 EDT 2010 · FEBS Lett.

DOI:https://doi.org/10.1016/j.febslet.2010.03.016· OSTI ID:1002348

Wielens, Jerome; Headey, Stephen J; Jeevarajah, Dharshini; Rhodes, David I; Deadman, John; Chalmers, David K; Scanlon, Martin J; Parker, Michael W ^[1]

---

1. SVIMR-A

HIV integrase (IN) is an essential enzyme in HIV replication and an important target for drug design. IN has been shown to interact with a number of cellular and viral proteins during the integration process. Disruption of these important interactions could provide a mechanism for allosteric inhibition of IN. We present the highest resolution crystal structure of the IN core domain to date. We also present a crystal structure of the IN core domain in complex with sucrose which is bound at the dimer interface in a region that has previously been reported to bind integrase inhibitors.

• Research Organization: Advanced Photon Source (APS), Argonne National Laboratory (ANL), Argonne, IL (US)
• Sponsoring Organization: USDOE
• OSTI ID: 1002348
• Journal Information: FEBS Lett., Journal Name: FEBS Lett. Journal Issue: (8) ; 04, 2010 Vol. 584; ISSN 0014-5793; ISSN FEBLAL
• Country of Publication: United States
• Language: ENGLISH

Related Subjects

36 MATERIALS SCIENCE
AIDS VIRUS
CRYSTAL STRUCTURE
DESIGN
DIMERS
ENZYMES
PROTEINS
RESOLUTION
SACCHAROSE
TARGETS