1vmp
From Proteopedia
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==Overview== | ==Overview== | ||
| - | We report the solution structure of the chemotactic cytokine (chemokine) | + | 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== | ==About this Structure== | ||
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[[Category: Human herpesvirus 4]] | [[Category: Human herpesvirus 4]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Liwang, A | + | [[Category: Liwang, A C.]] |
| - | [[Category: Liwang, P | + | [[Category: Liwang, P J.]] |
| - | [[Category: Peiper, S | + | [[Category: Peiper, S C.]] |
[[Category: Sun, Y.]] | [[Category: Sun, Y.]] | ||
| - | [[Category: Wang, Z | + | [[Category: Wang, Z X.]] |
[[Category: chemokine]] | [[Category: chemokine]] | ||
[[Category: herpesvirus]] | [[Category: herpesvirus]] | ||
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[[Category: vmip-ii]] | [[Category: vmip-ii]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:36:57 2008'' |
Revision as of 13:37, 21 February 2008
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STRUCTURE OF THE ANTI-HIV CHEMOKINE VMIP-II
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.
About this Structure
1VMP is a Single protein structure of sequence from Human herpesvirus 4. Full crystallographic information is available from OCA.
Reference
The solution structure of the anti-HIV chemokine vMIP-II., Liwang AC, Wang ZX, Sun Y, Peiper SC, Liwang PJ, Protein Sci. 1999 Nov;8(11):2270-80. PMID:10595530
Page seeded by OCA on Thu Feb 21 15:36:57 2008
Categories: Human herpesvirus 4 | Single protein | Liwang, A C. | Liwang, P J. | Peiper, S C. | Sun, Y. | Wang, Z X. | Chemokine | Herpesvirus | Hhv-8 | Kaposi's | Monomer | Sarcoma | Vmip-ii
