2e1x
NMR structure of the HIV-2 nucleocapsid protein
OverviewOverview
Nucleocapsid protein of HIV, containing two CCHC-type zinc fingers connected by a linker, is a multi-functional protein involved in many critical steps of the HIV life cycle. Several in vitro investigations demonstrated that the reactivities of the first zinc finger flanked by the linker of HIV-1 NCp7 and HIV-2 NCp8 were essential for binding to viral RNA, however, that of the second zinc finger flanked by the linker of NCp7 was very weak and non-specific, whereas the part of NCp8 called NCp8-f2, interacted strongly and specifically with viral RNA. In this study, the three-dimensional structure of NCp8-f2 was determined for the first time. Furthermore, we established that NCp8-f2 specifically binds to the stem-loop SD in viral RNA, and that the hydrophobic cleft and the basic residues close to the cleft were essential for specific binding to SD. We discuss the functional significance of NCp8-f2 for NCp8 being a multi-functional protein.
About this StructureAbout this Structure
2E1X is a Single protein structure. Full crystallographic information is available from OCA.
ReferenceReference
Structural role of the secondary active domain of HIV-2 NCp8 in multi-functionality., Matsui T, Kodera Y, Miyauchi E, Tanaka H, Endoh H, Komatsu H, Tanaka T, Kohno T, Maeda T, Biochem Biophys Res Commun. 2007 Jul 6;358(3):673-8. Epub 2007 May 4. PMID:17511966 Page seeded by OCA on Sun May 4 01:46:19 2008