Structure of SARS coronavirus spike receptor-binding domain complexed with receptor

被引：1499

作者：

Li, F

Li, WH

Farzan, M

Harrison, SC

机构：

[1] Harvard Univ, Sch Med, Dept Biol Chem & Mol Pharmacol, Boston, MA 02115 USA

[2] Childrens Hosp, Mol Med Lab, Boston, MA 02115 USA

[3] Childrens Hosp, Howard Hughes Med Inst, Boston, MA 02115 USA

[4] Harvard Univ, Sch Med, New England Primate Res Ctr, Dept Microbiol & Mol Genet, Southborough, MA 01772 USA

来源：

SCIENCE | 2005年 / 309卷 / 5742期

关键词：

D O I：

10.1126/science.1116480

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The spike protein (S) of SARS coronavirus (SARS-CoV) attaches the virus to its cellular receptor, angiotensin-converting enzyme 2 (ACE2). A defined receptor-binding domain (RBD) on S mediates this interaction. The crystal structure at 2.9 angstrom resolution of the RBD bound with the peptidase domain of human ACE2 shows that the RBD presents a gently concave surface, which cradles the N-terminal lobe of the peptidase. The atomic details at the interface between the two proteins clarify the importance of residue changes that facilitate efficient cross-species infection and human-to-human transmission. The structure of the RBD suggests ways to make truncated disulfide-stabilized RBD variants for use in the design of coronavirus vaccines.

引用

页码：1864 / 1868

页数：5

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