1DF4
INTERACTIONS BETWEEN HIV-1 GP41 CORE AND DETERGENTS AND THEIR IMPLICATIONS FOR MEMBRANE FUSION
1DF4 の概要
| エントリーDOI | 10.2210/pdb1df4/pdb |
| 関連するPDBエントリー | 1DF5 |
| 分子名称 | HIV-1 ENVELOPE GLYCOPROTEIN GP41 (2 entities in total) |
| 機能のキーワード | hiv-1, gp41, membrane fusion, protein-detergent interaction, viral protein |
| 由来する生物種 | Human immunodeficiency virus 1 詳細 |
| 細胞内の位置 | Transmembrane protein gp41: Virion membrane; Single-pass type I membrane protein. Surface protein gp120: Virion membrane; Peripheral membrane protein: P04578 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 7879.75 |
| 構造登録者 | |
| 主引用文献 | Shu, W.,Ji, H.,Lu, M. Interactions between HIV-1 gp41 core and detergents and their implications for membrane fusion. J.Biol.Chem., 275:1839-1845, 2000 Cited by PubMed Abstract: The gp41 envelope protein mediates entry of human immunodeficiency virus type 1 (HIV-1) into the cell by promoting membrane fusion. The crystal structure of a gp41 ectodomain core in its fusion-active state is a six-helix bundle in which a N-terminal trimeric coiled coil is surrounded by three C-terminal outer helices in an antiparallel orientation. Here we demonstrate that the N34(L6)C28 model of the gp41 core is stabilized by interaction with the ionic detergent sodium dodecyl sulfate (SDS) or the nonionic detergent n-octyl-beta-D-glucopyranoside (betaOG). The high resolution x-ray structures of N34(L6)C28 crystallized from two different detergent micellar media reveal a six-helix bundle conformation very similar to that of the molecule in water. Moreover, N34(L6)C28 adopts a highly alpha-helical conformation in lipid vesicles. Taken together, these results suggest that the six-helix bundle of the gp41 core displays substantial affinity for lipid bilayers rather than unfolding in the membrane environment. This characteristic may be important for formation of the fusion-active gp41 core structure and close apposition of the viral and cellular membranes for fusion. PubMed: 10636883DOI: 10.1074/jbc.275.3.1839 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.45 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード






