The solution structure of the anti-HIV chemokine vMIP-II.
The solution structure of the anti-HIV chemokine vMIP-II.
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抗HIV趋化因子vMIP-II的溶液结构。
DOI：
10.1110/ps.8.11.2270
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发表时间：
1999
期刊：
影响因子：
--
通讯作者：
Liwang,PJ
中科院分区：
文献类型：
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作者：
Liwang,AC;Wang,ZX;Sun,Y;Peiper,SC;Liwang,PJ
我们报告的溶液结构的趋化细胞因子（趋化因子）vMIP-Ⅱ。这种蛋白质具有独特的生物活性，因为它可以阻断几种不同的人类免疫缺陷病毒1型（HIV-1）毒株的感染。这是因为vMIP-II与广泛的趋化因子受体结合，其中一些被HIV用于获得细胞进入。vMIP-II是一种单体蛋白质，与趋化因子家族的大多数成员不同，其结构由无序的N-末端和螺旋转角（Gln 25-Leu 27）组成，螺旋转角（Gln 25-Leu 27）导致三链反平行β-折叠（Ser 29-Thr 34; Gly 42-Thr 47; Gln 52-Asp 56）的第一条链。折叠后是C-末端α-螺旋，从残基Asp 60延伸至Gln 68。C-末端螺旋以外的最后五个残基（Pro70-Arg 74）处于延伸构象，但这些C-末端残基中的几个与第一条β链接触。vMIP-II的结构相比，其他趋化因子，也阻止感染HIV-1，其缺乏能力形成二聚体的结构基础进行了讨论。
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 HIV 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 β-sheet (Ser29–Thr34; Gly42–Thr47; Gln52–Asp56). Following the sheet is a C-terminal α-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 β-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.