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2EC7

Solution Structure of Human Immunodificiency Virus Type-2 Nucleocapsid Protein

2EC7 の概要
エントリーDOI10.2210/pdb2ec7/pdb
関連するPDBエントリー1NC8 2DI2 2E1X
NMR情報BMRB: 7384
分子名称Gag polyprotein (Pr55Gag), ZINC ION (2 entities in total)
機能のキーワードnucleocapsid protein, hiv-2, rna recognition, zinc finger, viral protein
由来する生物種Human immunodeficiency virus type 2 (ISOLATE GHANA-1)
タンパク質・核酸の鎖数1
化学式量合計5698.36
構造登録者
Matsui, T.,Kodera, Y.,Tanaka, T.,Endoh, H.,Tanaka, H.,Miyauchi, E.,Komatsu, H.,Kohno, T.,Maeda, T. (登録日: 2007-02-10, 公開日: 2008-02-19, 最終更新日: 2024-05-01)
主引用文献Matsui, T.,Tanaka, T.,Endoh, H.,Sato, K.,Tanaka, H.,Miyauchi, E.,Kawashima, Y.,Nagai-Makabe, M.,Komatsu, H.,Kohno, T.,Maeda, T.,Kodera, Y.
The RNA recognition mechanism of human immunodeficiency virus (HIV) type 2 NCp8 is different from that of HIV-1 NCp7
Biochemistry, 48:4314-4323, 2009
Cited by
PubMed Abstract: The nucleocapsid (NC) protein of HIV, which contains two CCHC-type zinc fingers connected by a linker, is a multifunctional protein involved in many of the critical steps of the HIV life cycle. HIV-1 and HIV-2 contain NC proteins NCp7 and NCp8, respectively. The amino acid sequences of both NC proteins are 67% identical. For NCp7, the important elements for RNA binding were found to be the first zinc finger flanked by the linker, as the minimal active domain, and the 3(10) helix in the N-terminus, as the secondary active domain. However, for the NCp8 counterpart in HIV-2, the mechanism for binding to viral RNA has not yet been clarified. In this study, we determined NCp8's three-dimensional structure for the first time and examined the dynamic behavior and chemical shift perturbation as a function of the concentration of viral RNA SL3. Moreover, the specific binding activities of NCp8 and the NCp8-derived peptides with SL3 were examined by a native polyacrylamide gel electrophoresis assay. These results indicate that the RNA recognition mechanism for NCp8 is different from that of NCp7 and that the hydrophobic cleft in the second zinc finger acts as a secondary active domain instead of the 3(10) helix in NCp7. Furthermore, the flexibility of the linker is limited by the hydrogen bond between the first zinc finger (Asn11) and the linker (Arg27), which makes it possible for the sites around Trp10 in the minimal active domain and the secondary active domain to form the binding surface.
PubMed: 19334676
DOI: 10.1021/bi802364b
主引用文献が同じPDBエントリー
実験手法
SOLUTION NMR
構造検証レポート
Validation report summary of 2ec7
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-07-09に公開中

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