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

ABSTRACT: 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.

SUBMITTER: Tan K

PROVIDER: S-EPMC125375 | biostudies-literature | 2002 May

REPOSITORIES: biostudies-literature

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

Tan Kemin K Zelus Bruce D BD Meijers Rob R Liu Jin-huan JH Bergelson Jeffrey M JM Duke Norma N Zhang Rongguang R Joachimiak Andrzej A Holmes Kathryn V KV Wang Jia-huai JH

The EMBO journal 20020501 9

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 proto ...[more]

PMID: 11980704

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