1vmp: Difference between revisions

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==Overview==

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.

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.

==About this Structure==

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[[Category: Human herpesvirus 4]]

[[Category: Single protein]]

[[Category: Liwang, A.C.]]

[[Category: Liwang, A C.]]

[[Category: Liwang, P.J.]]

[[Category: Liwang, P J.]]

[[Category: Peiper, S.C.]]

[[Category: Peiper, S C.]]

[[Category: Sun, Y.]]

[[Category: Wang, Z.X.]]

[[Category: Wang, Z X.]]

[[Category: chemokine]]

[[Category: herpesvirus]]

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[[Category: vmip-ii]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-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.
+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.
 ==About this Structure==
@@ Line 13: / Line 13: @@
 [[Category: Human herpesvirus 4]]
 [[Category: Single protein]]
-[[Category: Liwang, A.C.]]
+[[Category: Liwang, A C.]]
-[[Category: Liwang, P.J.]]
+[[Category: Liwang, P J.]]
-[[Category: Peiper, S.C.]]
+[[Category: Peiper, S C.]]
 [[Category: Sun, Y.]]
-[[Category: Wang, Z.X.]]
+[[Category: Wang, Z X.]]
 [[Category: chemokine]]
 [[Category: herpesvirus]]
@@ Line 26: / Line 26: @@
 [[Category: vmip-ii]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:05:10 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:36:57 2008''