1df4: Difference between revisions

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</StructureSection>
</StructureSection>
[[Category: Human immunodeficiency virus 1]]
[[Category: Human immunodeficiency virus 1]]
[[Category: Ji, H.]]
[[Category: Ji, H]]
[[Category: Lu, M.]]
[[Category: Lu, M]]
[[Category: Shu, W.]]
[[Category: Shu, W]]
[[Category: Gp41]]
[[Category: Gp41]]
[[Category: Hiv-1]]
[[Category: Hiv-1]]

Revision as of 00:05, 23 December 2014

INTERACTIONS BETWEEN HIV-1 GP41 CORE AND DETERGENTS AND THEIR IMPLICATIONS FOR MEMBRANE FUSIONINTERACTIONS BETWEEN HIV-1 GP41 CORE AND DETERGENTS AND THEIR IMPLICATIONS FOR MEMBRANE FUSION

Structural highlights

1df4 is a 1 chain structure with sequence from Human immunodeficiency virus 1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, OCA, RCSB, PDBsum

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

Interactions between HIV-1 gp41 core and detergents and their implications for membrane fusion.,Shu W, Ji H, Lu M J Biol Chem. 2000 Jan 21;275(3):1839-45. PMID:10636883[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Shu W, Ji H, Lu M. Interactions between HIV-1 gp41 core and detergents and their implications for membrane fusion. J Biol Chem. 2000 Jan 21;275(3):1839-45. PMID:10636883

1df4, resolution 1.45Å

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OCA