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PDBsum entry 1vmp
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Antiviral protein
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PDB id
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1vmp
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Contents |
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* Residue conservation analysis
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DOI no:
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Protein Sci
8:2270-2280
(1999)
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PubMed id:
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The solution structure of the anti-HIV chemokine vMIP-II.
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A.C.Liwang,
Z.X.Wang,
Y.Sun,
S.C.Peiper,
P.J.Liwang.
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ABSTRACT
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We report the solution structure of the chemotactic cytokine (chemokine)
vMIP-II. This protein has unique biological activities in that it blocks
infection by several different human immunodeficiency virus type 1 (HIV-1)
strains. This occurs because vMIP-II binds to a wide range of chemokine
receptors, some of which are used by HJV to gain cell entry. vMIP-II is a
monomeric protein, unlike most members of the chemokine family, and its
structure consists of a disordered N-terminus, followed by a helical turn
(Gln25-Leu27), which leads into the first strand of a three-stranded
antiparallel beta-sheet (Ser29-Thr34; Gly42-Thr47; Gln52-Asp56). Following the
sheet is a C-terminal alpha-helix, which extends from residue Asp60 until Gln68.
The final five residues beyond the C-terminal helix (Pro70-Arg74) are in an
extended conformation, but several of these C-terminal residues contact the
first beta-strand. The structure of vMIP-II is compared to other chemokines that
also block infection by HIV-1, and the structural basis of its lack of ability
to form a dimer is discussed.
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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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D.Liu,
N.Madani,
Y.Li,
R.Cao,
W.T.Choi,
S.P.Kawatkar,
M.Y.Lim,
S.Kumar,
C.Z.Dong,
J.Wang,
J.D.Russell,
C.R.Lefebure,
J.An,
S.Wilson,
Y.G.Gao,
L.A.Pallansch,
J.G.Sodroski,
and
Z.Huang
(2007).
Crystal structure and structural mechanism of a novel anti-human immunodeficiency virus and D-amino acid-containing chemokine.
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J Virol,
81,
11489-11498.
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S.J.Allen,
S.E.Crown,
and
T.M.Handel
(2007).
Chemokine: receptor structure, interactions, and antagonism.
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Annu Rev Immunol,
25,
787-820.
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T.Gao,
X.Zhang,
N.B.Ivleva,
S.S.Golden,
and
A.LiWang
(2007).
NMR structure of the pseudo-receiver domain of CikA.
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Protein Sci,
16,
465-475.
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PDB code:
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C.Baysal,
and
A.R.Atilgan
(2001).
Elucidating the structural mechanisms for biological activity of the chemokine family.
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Proteins,
43,
150-160.
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S.A.Smith,
and
G.J.Kotwal
(2001).
Virokines: novel immunomodulatory agents.
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Expert Opin Biol Ther,
1,
343-357.
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W.Shao,
E.Fernandez,
A.Sachpatzidis,
J.Wilken,
D.A.Thompson,
B.I.Schweitzer,
and
E.Lolis
(2001).
CCR2 and CCR5 receptor-binding properties of herpesvirus-8 vMIP-II based on sequence analysis and its solution structure.
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Eur J Biochem,
268,
2948-2959.
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PDB code:
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E.J.Fernandez,
J.Wilken,
D.A.Thompson,
S.C.Peiper,
and
E.Lolis
(2000).
Comparison of the structure of vMIP-II with eotaxin-1, RANTES, and MCP-3 suggests a unique mechanism for CCR3 activation.
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Biochemistry,
39,
12837-12844.
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PDB code:
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Z.Luo,
X.Fan,
N.Zhou,
M.Hiraoka,
J.Luo,
H.Kaji,
and
Z.Huang
(2000).
Structure-function study and anti-HIV activity of synthetic peptide analogues derived from viral chemokine vMIP-II.
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Biochemistry,
39,
13545-13550.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
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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Links
