1VMP

STRUCTURE OF THE ANTI-HIV CHEMOKINE VMIP-II

Summary for 1VMP

• Entry DOI: 10.2210/pdb1vmp/pdb
• Descriptor: PROTEIN (ANTI-HIV CHEMOKINE MIP VII) (1 entity in total)
• Functional Keywords: vmip-ii, chemokine, monomer, sarcoma, herpesvirus, hhv-8, kaposi's, antiviral protein
• Biological source: Human herpesvirus 8
• Cellular location: Secreted: Q98157
• Total number of polymer chains: 1
• Total formula weight: 8142.66

Authors

Liwang, A.C.,Wang, Z.-X.,Sun, Y.,Peiper, S.C.,Liwang, P.J. (deposition date: 1999-03-25, release date: 1999-11-24, Last modification date: 2024-11-20)

Primary citation

Liwang, A.C.,Wang, Z.X.,Sun, Y.,Peiper, S.C.,Liwang, P.J.
The solution structure of the anti-HIV chemokine vMIP-II.
Protein Sci., 8:2270-2280, 1999

PubMed Abstract: 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.

PubMed: 10595530

Experimental method

SOLUTION NMR