1DF5
INTERACTIONS BETWEEN HIV-1 GP41 CORE AND DETERGENTS AND THEIR IMPLICATIONS FOR MEMBRANE FUSION
Summary for 1DF5
Entry DOI | 10.2210/pdb1df5/pdb |
Related | 1DF4 |
Descriptor | HIV-1 ENVELOPE GLYCOPROTEIN GP41 (1 entity in total) |
Functional Keywords | hiv-1, gp41, membrane fusion, protein-detergent interaction, viral protein |
Biological source | Human immunodeficiency virus 1 More |
Cellular location | Transmembrane protein gp41: Virion membrane; Single-pass type I membrane protein. Surface protein gp120: Virion membrane; Peripheral membrane protein: P04578 |
Total number of polymer chains | 1 |
Total formula weight | 7879.75 |
Authors | |
Primary citation | 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 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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