CRYSTAL-STRUCTURE OF THE PRINCIPAL NEUTRALIZATION SITE OF HIV-1
CRYSTAL-STRUCTURE OF THE PRINCIPAL NEUTRALIZATION SITE OF HIV-1
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DOI：
10.1126/science.7511253
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发表时间：
1994-04-01
期刊：
影响因子：
56.9
通讯作者：
WILSON, IA
中科院分区：
文献类型：
--
作者：
GHIARA, JB;STURA, EA;WILSON, IA
从第三个变量（V3）环中，人类免疫缺陷病毒型1（HIV-1）GP120和广泛中和抗体（59.1）的Fab片段的晶体结构（V3）环（V3）环。 Angstrom分辨率。包含Gly-Pro-Gly-Arg-Ala-Phe序列的V3环的尖端采用双向构象，这可能是许多HIV-1分离株中其保护的基础。 HIV-1主中和决定因素的完整图是通过将V3环肽的结构缝合在一起结合到59.1的结构，并与中和抗体中和抗体结合的结构（50.1）。重叠表位的结构保护表明，这种与生物学相关的构象可以用于合成疫苗和药物的设计，以抑制HIV-1进入和病毒相关的细胞融合。
The crystal structure of a complex between a 24-amino acid peptide from the third variable (V3) loop of human immunodeficiency virus-type 1 (HIV-1) gp120 and the Fab fragment of a broadly neutralizing antibody (59.1) was determined to 3 angstrom resolution. The tip of the V3 loop containing the Gly-Pro-Gly-Arg-Ala-Phe sequence adopts a double-turn conformation, which may be the basis ot its conservation in many HIV-1 isolates. A complete map of the HIV-1 principal neutralizing determinant was constructed by stitching together structures of V3 loop peptides bound to 59.1 and to an isolate-specific (MN) neutralizing antibody (50.1). Structural conservation of the overlapping epitopes suggests that this biologically relevant conformation could be of use in the design of synthetic vaccines and drugs to inhibit HIV-1 entry and virus-related cellular fusion.