Crystal structure of murine coronavirus receptor sCEACAM1a[1,4],a member of the carcinoembtyonic antigen family

Journal Article · Wed May 01 04:00:00 EDT 2002 · Embo J.

DOI:https://doi.org/10.1093/emboj/21.9.2076· OSTI ID:961026

Tan, K; Zelus, B D; Meijers, R; Liu, J -H; Bergelson, J M; Zhang, R; Duke, N; Joachimiak, A; Holmes, K V; Wang, J -H

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.

• Research Organization: Argonne National Laboratory (ANL)
• Sponsoring Organization: NIH
• DOE Contract Number: AC02-06CH11357
• OSTI ID: 961026
• Report Number(s): ANL/BIO/JA-43934
• Journal Information: Embo J., Journal Name: Embo J. Journal Issue: 9 ; May 1, 2002 Vol. 21; ISSN EMJODG; ISSN 0261-4189
• Country of Publication: United States
• Language: ENGLISH

Related Subjects

36 MATERIALS SCIENCE
AMINO ACID SEQUENCE
ANTIGENS
ARCHITECTURE
CARCINOEMBRYONIC ANTIGEN
CRYSTAL STRUCTURE
GLYCOPROTEINS
HEPATITIS
HUMAN POPULATIONS
INTERACTIONS
MICE
PROTEIN STRUCTURE
PROTEINS
RECEPTORS
RESIDUES