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* Residue conservation analysis
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DOI no:
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Proc Natl Acad Sci U S A
95:9134-9139
(1998)
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PubMed id:
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Crystal structure of the simian immunodeficiency virus (SIV) gp41 core: conserved helical interactions underlie the broad inhibitory activity of gp41 peptides.
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V.N.Malashkevich,
D.C.Chan,
C.T.Chutkowski,
P.S.Kim.
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ABSTRACT
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The gp41 subunit of the envelope protein complex from human and simian
immunodeficiency viruses (HIV and SIV) mediates membrane fusion during viral
entry. The crystal structure of the HIV-1 gp41 ectodomain core in its proposed
fusion-active state is a six-helix bundle. Here we have reconstituted the core
of the SIV gp41 ectodomain with two synthetic peptides called SIV N36 and SIV
C34, which form a highly helical trimer of heterodimers. The 2.2 A resolution
crystal structure of this SIV N36/C34 complex is very similar to the analogous
structure in HIV-1 gp41. In both structures, three N36 helices form a central
trimeric coiled coil. Three C34 helices pack in an antiparallel orientation into
highly conserved, hydrophobic grooves along the surface of this coiled coil. The
conserved nature of the N36-C34 interface suggests that the HIV-1 and SIV
peptides are functionally interchangeable. Indeed, a heterotypic complex between
HIV-1 N36 and SIV C34 peptides is highly helical and stable. Moreover, as with
HIV-1 C34, the SIV C34 peptide is a potent inhibitor of HIV-1 infection. These
results identify conserved packing interactions between the N and C helices of
gp41 and have implications for the development of C peptide analogs with broad
inhibitory activity.
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Selected figure(s)
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Figure 1.
Fig. 1. A schematic view of gp41, showing the locations
of the N36 and C34 peptides from SIV and HIV-1. Identical
residues between the SIV and HIV-1 peptides are indicated with a
bar, and similar residues are indicated by dots. To facilitate
comparisons between the HIV-1 and SIV structures, the peptide
residues are numbered according to their positions in HIV-1
gp160 (HXB2 strain; GenBank accession no. K03455). For the SIV
peptides (SIV Mac239 strain; GenBank accession no. M33262), N36
actually corresponds to positions 559-594, and C34 corresponds
to 637-670. The 4,3 hydrophobic repeats are indicated with black
shading. FP, fusion peptide; S---S, disulfide bond; TM,
transmembrane region; CYTO, cytoplasmic domain.
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Figure 5.
Fig. 5. The conserved hydrophobic cavity on the surface
of the N36 coiled coil. (A) Structural overlay of the published
HIV-1 gp41 ectodomain structures. The three structures [Chan et
al. (5), yellow; Weissenhorn et al. (6), red; and Tan et al.
(7), green] deviate substantially in this region. (B)
Interactions in the N36 hydrophobic cavity of SIV (blue) are
most similar to the Chan et al. (5) HIV-1 structure (yellow).
The same superposition as in Fig. 4 A and B was used. The SIV
N36 coiled coil is represented as a molecular surface, and the
C34 helices are shown as ribbons with selected side chains. The
molecular surface is colored white for residues that are
identical in SIV and HIV, and green for residues that are not
identical. Figures were generated with GRASP (28).
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Figures were
selected
by an automated process.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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Biochemistry,
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PDB code:
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M.Lu,
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J Virol,
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PDB codes:
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R.J.Center,
P.Schuck,
R.D.Leapman,
L.O.Arthur,
P.L.Earl,
B.Moss,
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(2001).
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Proc Natl Acad Sci U S A,
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(2001).
The trimer-of-hairpins motif in membrane fusion: Visna virus.
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Proc Natl Acad Sci U S A,
98,
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PDB code:
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W.E.Johnson,
J.M.Sauvron,
and
R.C.Desrosiers
(2001).
Conserved, N-linked carbohydrates of human immunodeficiency virus type 1 gp41 are largely dispensable for viral replication.
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J Virol,
75,
11426-11436.
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A.L.Maerz,
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Functional implications of the human T-lymphotropic virus type 1 transmembrane glycoprotein helical hairpin structure.
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J Virol,
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H.Ji,
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and
M.Lu
(2000).
Buried polar interactions and conformational stability in the simian immunodeficiency virus (SIV) gp41 core.
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Biochemistry,
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676-685.
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J.K.Ghosh,
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Sendai virus internal fusion peptide: structural and functional characterization and a plausible mode of viral entry inhibition.
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The core of the respiratory syncytial virus fusion protein is a trimeric coiled coil.
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J Virol,
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Heptad-repeat regions of respiratory syncytial virus F1 protein form a six-membered coiled-coil complex.
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Biochemistry,
39,
11684-11695.
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S.Watanabe,
A.Takada,
T.Watanabe,
H.Ito,
H.Kida,
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(2000).
Functional importance of the coiled-coil of the Ebola virus glycoprotein.
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J Virol,
74,
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W.Shu,
J.Liu,
H.Ji,
L.Radigen,
S.Jiang,
and
M.Lu
(2000).
Helical interactions in the HIV-1 gp41 core reveal structural basis for the inhibitory activity of gp41 peptides.
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Biochemistry,
39,
1634-1642.
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PDB code:
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W.Wickner,
and
A.Haas
(2000).
Yeast homotypic vacuole fusion: a window on organelle trafficking mechanisms.
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Annu Rev Biochem,
69,
247-275.
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X.Zhao,
M.Singh,
V.N.Malashkevich,
and
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(2000).
Structural characterization of the human respiratory syncytial virus fusion protein core.
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Proc Natl Acad Sci U S A,
97,
14172-14177.
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PDB code:
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Y.Weng,
Z.Yang,
and
C.D.Weiss
(2000).
Structure-function studies of the self-assembly domain of the human immunodeficiency virus type 1 transmembrane protein gp41.
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J Virol,
74,
5368-5372.
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B.Kobe,
R.J.Center,
B.E.Kemp,
and
P.Poumbourios
(1999).
Crystal structure of human T cell leukemia virus type 1 gp21 ectodomain crystallized as a maltose-binding protein chimera reveals structural evolution of retroviral transmembrane proteins.
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Proc Natl Acad Sci U S A,
96,
4319-4324.
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PDB code:
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D.H.Kingsley,
A.Behbahani,
A.Rashtian,
G.W.Blissard,
and
J.Zimmerberg
(1999).
A discrete stage of baculovirus GP64-mediated membrane fusion.
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Mol Biol Cell,
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4191-4200.
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J.C.Beauchamp,
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Methods for X-ray diffraction analysis of macromolecular structures.
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Curr Opin Chem Biol,
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K.A.Baker,
R.E.Dutch,
R.A.Lamb,
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T.S.Jardetzky
(1999).
Structural basis for paramyxovirus-mediated membrane fusion.
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| |
Mol Cell,
3,
309-319.
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PDB code:
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M.Caffrey,
J.Kaufman,
S.Stahl,
P.Wingfield,
A.M.Gronenborn,
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(1999).
Monomer-trimer equilibrium of the ectodomain of SIV gp41: insight into the mechanism of peptide inhibition of HIV infection.
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Protein Sci,
8,
1904-1907.
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R.Jahn,
and
T.C.Südhof
(1999).
Membrane fusion and exocytosis.
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Annu Rev Biochem,
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863-911.
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S.L.Allison,
K.Stiasny,
K.Stadler,
C.W.Mandl,
and
F.X.Heinz
(1999).
Mapping of functional elements in the stem-anchor region of tick-borne encephalitis virus envelope protein E.
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J Virol,
73,
5605-5612.
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V.N.Malashkevich,
B.J.Schneider,
M.L.McNally,
M.A.Milhollen,
J.X.Pang,
and
P.S.Kim
(1999).
Core structure of the envelope glycoprotein GP2 from Ebola virus at 1.9-A resolution.
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Proc Natl Acad Sci U S A,
96,
2662-2667.
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PDB code:
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D.C.Chan,
C.T.Chutkowski,
and
P.S.Kim
(1998).
Evidence that a prominent cavity in the coiled coil of HIV type 1 gp41 is an attractive drug target.
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Proc Natl Acad Sci U S A,
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S.Jiang,
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A conformation-specific monoclonal antibody reacting with fusion-active gp41 from the human immunodeficiency virus type 1 envelope glycoprotein.
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J Virol,
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W.Weissenhorn,
A.Carfí,
K.H.Lee,
J.J.Skehel,
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(1998).
Crystal structure of the Ebola virus membrane fusion subunit, GP2, from the envelope glycoprotein ectodomain.
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Mol Cell,
2,
605-616.
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PDB code:
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so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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