1vmp

From Proteopedia

Revision as of 15:05, 15 February 2008

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

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