Rizzuto C, Sodroski J
Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, Boston, Massachusetts 02115, USA.
AIDS Res Hum Retroviruses. 2000 May 20;16(8):741-9. doi: 10.1089/088922200308747.
A previous study implicated a conserved surface of the human immunodeficiency virus (HIV-1) gp120 exterior envelope glycoprotein in binding the CCR5 viral coreceptor (Rizzuto C, Wyatt R, Hernández-Ramos N, Sun Y, Kwong PD, Hendrickson WA, and Sodroski J: Science 1998;280:1949-1953). Additional mutagenesis indicates that important residues in this region for CCR5 binding are Ile-420, Lys-421, Gln-422, Pro-438, and Gly-441. These highly conserved residues are located on two strands that connect the gp120 bridging sheet and outer domain, suggesting a mechanism whereby interdomain conformational shifts induced by CD4 binding could facilitate CCR5 binding.
先前的一项研究表明,人类免疫缺陷病毒(HIV-1)外膜糖蛋白gp120的一个保守表面参与了与CCR5病毒共受体的结合(里祖托C、怀亚特R、埃尔南德斯-拉莫斯N、孙Y、邝沛东、亨德里克森WA和索德罗斯基J:《科学》,1998年;280:1949 - 1953)。进一步的诱变表明,该区域中对于CCR5结合重要的残基是异亮氨酸-420、赖氨酸-421、谷氨酰胺-422、脯氨酸-438和甘氨酸-441。这些高度保守的残基位于连接gp120桥接片层和外结构域的两条链上,提示一种机制,即由CD4结合诱导的结构域间构象变化可能促进CCR5的结合。