2e1x

From Proteopedia

Revision as of 12:59, 23 January 2008

NMR structure of the HIV-2 nucleocapsid protein

Overview

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 Structure

2E1X is a Single protein structure of sequence from [1] with as ligand. Full crystallographic information is available from OCA.

Reference

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

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