2GK2

Crystal structure of the N terminal domain of human CEACAM1

Summary for 2GK2

• Entry DOI: 10.2210/pdb2gk2/pdb
• Descriptor: Carcinoembryonic antigen-related cell adhesion molecule 1, NICKEL (II) ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: immunoglobulin domain, adhesion protein, cell adhesion
• Biological source: Homo sapiens (human)
• Cellular location: Isoform 1: Cell membrane ; Single-pass type I membrane protein . Isoform 2: Secreted . Isoform 3: Secreted . Isoform 4: Secreted . Isoform 5: Cell membrane; Single-pass type I membrane protein. Isoform 6: Cell membrane; Single-pass type I membrane protein. Isoform 7: Cell membrane; Single-pass type I membrane protein. Isoform 8: Cell membrane ; Single-pass type I membrane protein . Cell projection, microvillus membrane ; Single-pass type I membrane protein : P13688
• Total number of polymer chains: 2
• Total formula weight: 24736.53

Authors

Fedarovich, A.,Tomberg, J.,Nicholas, R.A.,Davies, C. (deposition date: 2006-03-31, release date: 2006-09-05, Last modification date: 2023-08-30)

Primary citation

Fedarovich, A.,Tomberg, J.,Nicholas, R.A.,Davies, C.
Structure of the N-terminal domain of human CEACAM1: binding target of the opacity proteins during invasion of Neisseria meningitidis and N. gonorrhoeae.
Acta Crystallogr.,Sect.D, 62:971-979, 2006

PubMed Abstract: CEACAM1 is a cellular adhesion molecule whose protein expression is down-regulated in several carcinomas and which also contributes to the pathogenicity of Neisseria by acting as a receptor for Opa proteins. The crystal structure of the N-terminal (D1) domain of human CEACAM1 has been determined at 2.2 Angstrom resolution. The structure shows several differences compared with a lower resolution model of the same domain from mouse solved previously, especially in the functional regions. Mapping of the sites of mutations that lower or abolish the binding of CEACAM1 to Opa proteins shows a distinct clustering of residues on the GFCC'C'' face of the molecule. Prominent amongst these are residues in the C, C' and F strands and the CC' loop. A similar analysis shows that the region responsible for homophilic or heterophilic interactions of CEACAM1 is also on the GFCC'C'' face and overlaps partially with the Opa-binding region. This higher resolution structure of CEACAM1 will facilitate a more precise dissection of its functional regions in the context of neisserial pathogenesis, cellular adhesion and immune evasion.

PubMed: 16929097
DOI: 10.1107/S0907444906020737

Experimental method

X-RAY DIFFRACTION (2.2 Å)