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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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References listed in PDB file
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Key reference
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Title
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The solution structure of the anti-Hiv chemokine vmip-Ii.
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Authors
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A.C.Liwang,
Z.X.Wang,
Y.Sun,
S.C.Peiper,
P.J.Liwang.
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Ref.
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Protein Sci, 1999,
8,
2270-2280.
[DOI no: ]
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PubMed id
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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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