Crystal structure of murine sCEACAM1a[1,4]: a coronavirus receptor in the CEA family

被引：95

作者：

Tan, KM

Zelus, BD

Meijers, R

Liu, JH

Bergelson, JM

Duke, N

Zhang, R

Joachimiak, A

Holmes, KV

Wang, JH ^{[1
]}

机构：

[1] Univ Colorado, Hlth Sci Ctr, Dept Microbiol, 4200 E 9th Ave, Denver, CO 80262 USA

[2] Dana Farber Canc Inst, Boston, MA 02115 USA

[3] Harvard Univ, Sch Med, Dept Med, Cambridge, MA 02138 USA

[4] Harvard Univ, Sch Med, Dept Pediat, Cambridge, MA 02138 USA

[5] Harvard Univ, Sch Med, Dept Biol Chem & Mol Pharmacol, Cambridge, MA 02138 USA

[6] Univ Penn, Childrens Hosp Philadelphia, Sch Med, Philadelphia, PA 19104 USA

[7] Argonne Natl Lab, Biosci Div, Argonne, IL 60439 USA

来源：

EMBO JOURNAL | 2002年 / 21卷 / 09期

关键词：

bacterial binding; CEA family; cell adhesion; coronavirus receptor; crystal structure;

D O I：

10.1093/emboj/21.9.2076

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

CEACAM1 is a member of the carcinoembryonic antigen (CEA) family. Isoforms of murine CEACAM1 serve as receptors for mouse hepatitis virus (MHV), a murine coronavirus. Here we report the crystal structure of soluble murine sCEACAM1a[1,4], which is composed of two Ig-like domains and has MHV neutralizing activity. Its N-terminal domain has a uniquely folded CC' loop that encompasses key virus-binding residues. This is the first atomic structure of any member of the CEA family, and provides a prototypic architecture for functional exploration of CEA family members. We discuss the structural basis of virus receptor activities of murine CEACAM1 proteins, binding of Neisseria to human CEACAM1, and other homophilic and heterophilic interactions of CEA family members.

引用

页码：2076 / 2086

页数：11

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