1df4: Difference between revisions

Revision as of 13:15, 21 February 2008

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

OverviewOverview

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.

About this StructureAbout this Structure

1DF4 is a Single protein structure of sequence from Human immunodeficiency virus 1. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Thu Feb 21 12:15:59 2008

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OCA

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-[[Image:1df4.gif|left|200px]]<br />
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 caption="1df4, resolution 1.45&Aring;" />
 '''INTERACTIONS BETWEEN HIV-1 GP41 CORE AND DETERGENTS AND THEIR IMPLICATIONS FOR MEMBRANE FUSION'''<br />
 ==Overview==
-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.
+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.
 ==About this Structure==
-DF4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DF4 OCA].
+DF4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DF4 OCA].
 ==Reference==
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 [[Category: protein-detergent interaction]]
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