2E1X
NMR structure of the HIV-2 nucleocapsid protein
Summary for 2E1X
| Entry DOI | 10.2210/pdb2e1x/pdb |
| Descriptor | Gag-Pol polyprotein (Pr160Gag-Pol), ZINC ION (2 entities in total) |
| Functional Keywords | nucleocapsid protein, hiv-2, rna recognition, zinc finger, viral protein |
| Cellular location | Matrix protein p17: Virion (Potential). Capsid protein p24: Virion (Potential). Nucleocapsid protein p7: Virion (Potential). Reverse transcriptase/ribonuclease H: Virion (Potential). Integrase: Virion (Potential): P18042 |
| Total number of polymer chains | 1 |
| Total formula weight | 3085.99 |
| Authors | Matsui, T.,Kodera, Y.,Miyauchi, E.,Tanaka, H.,Endoh, H.,Komatsu, H.,Tanaka, T.,Kohno, T.,Maeda, T. (deposition date: 2006-11-03, release date: 2007-06-05, Last modification date: 2024-11-13) |
| Primary citation | Matsui, T.,Kodera, Y.,Miyauchi, E.,Tanaka, H.,Endoh, H.,Komatsu, H.,Tanaka, T.,Kohno, T.,Maeda, T. Structural role of the secondary active domain of HIV-2 NCp8 in multi-functionality Biochem.Biophys.Res.Commun., 358:673-678, 2007 Cited by PubMed Abstract: 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. PubMed: 17511966DOI: 10.1016/j.bbrc.2007.04.141 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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