PDBsum entry: 1l6z

Cell adhesion

PDB id: 1l6z

Contents

Protein chain

203 a.a. *

Ligands

NDG

NAG ×2

NAG-NAG-BMA

Waters ×26

* Residue conservation analysis

PDB id:

1l6z

Name:

Cell adhesion

Title:

Crystal structure of murine ceacam1a[1,4]: a coronavirus rec cell adhesion molecule in the cea family

Structure:

Biliary glycoprotein c. Chain: a. Synonym: biliary glycoprotein c, cd66a. Engineered: yes

Source:

Mus musculus. House mouse. Organism_taxid: 10090. Gene: murine ceacam1a. Expressed in: cricetulus griseus. Expression_system_taxid: 10029. Expression_system_cell: ovary cells.

Resolution:

3.32Å R-factor: 0.295 R-free: 0.329

Authors:

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

Key ref:

K.Tan et al. (2002). Crystal structure of murine sCEACAM1a[1,4]: a coronavirus receptor in the CEA family. EMBO J, 21, 2076-2086. PubMed id: 11980704 DOI: 10.1093/emboj/21.9.2076

Date:

14-Mar-02 Release date: 14-Sep-02

Protein chain

P31809  (CEAM1_MOUSE) -  Carcinoembryonic antigen-related cell adhesion molecule 1

Seq: 521 a.a.

Struc: 203 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 

• Biochemical function: protein binding (1 term)

DOI no: 10.1093/emboj/21.9.2076

EMBO J 21:2076-2086 (2002)

PubMed id: 11980704

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

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

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.

Selected figure(s)

Figure 1.
Figure 1 Stereo view of the ribbon drawing of msCEACAM1a[1,4], which contains two Ig-like domains. The CC' loop in the N-terminal domain (D1), which is involved in binding of MHV and other ligands, is highlighted in yellow. The predicted key virus-binding residue Ile41 on the CC' loop is shown in red in ball-and-stick representation. The FG loop of D1, another biologically important element, is shown in violet. The carbohydrate moieties are drawn in gray in ball-and-stick representation. The glycan at Asn70 that is conserved in the whole CEA family is labeled. The figure was prepared using MOLSCRIPT (Kraulis, 1991).

Figure 3.
Figure 3 A comparative view of structures of several virus receptors, including: msCEACAM1a, the receptor for murine coronavirus MHV; ICAM1, the receptor for the major group of rhinoviruses; CD4, the primary receptor for HIV; and CD46, the receptor for measles virus. Only their N-terminal domains are shown here. The key virus-binding motifs with unique topological features are highlighted in red.

The above figures are reprinted from an Open Access publication published by Macmillan Publishers Ltd: EMBO J (2002, 21, 2076-2086) copyright 2002.

Figures were selected by the author.