The solution structure of the anti-HIV chemokine vMIP-II.
Publication/Presentation Date
11-1-1999
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.
Volume
8
Issue
11
First Page
2270
Last Page
2280
ISSN
0961-8368
Published In/Presented At
Liwang, A. C., Wang, Z. X., Sun, Y., Peiper, S. C., & Liwang, P. J. (1999). The solution structure of the anti-HIV chemokine vMIP-II. Protein science : a publication of the Protein Society, 8(11), 2270–2280. https://doi.org/10.1110/ps.8.11.2270
Disciplines
Business Administration, Management, and Operations | Health and Medical Administration | Management Sciences and Quantitative Methods
PubMedID
10595530
Department(s)
Administration and Leadership
Document Type
Article