PDBsum entry 4y89

Cell adhesion

PDB id

4y89

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Contents

			Protein chains

					109 a.a.

			Metals

					_CL ×3

			Waters ×269

PDB id:

4y89

Links

Name:

Cell adhesion

Title:

Crystal structure of the n-terminal domain of ceacam7

Structure:

Carcinoembryonic antigen-related cell adhesion molecule 7. Chain: a, b, c, d. Fragment: igv domain (unp residues 34-142). Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: ceacam7. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

1.47Å

R-factor:

0.146

R-free:

0.193

Authors:

D.A.Bonsor,E.J.Sundberg

Key ref:

D.A.Bonsor et al. (2015). Structure of the N-terminal dimerization domain of CEACAM7. Acta Crystallogr F Struct Biol Commun, 71, 1169-1175. PubMed id: 26323304 DOI: 10.1107/S2053230X15013576

Date:

16-Feb-15

Release date:

02-Sep-15

PROCHECK

	Headers

	References

Protein chains

Q14002 (CEAM7_HUMAN) - Carcinoembryonic antigen-related cell adhesion molecule 7 from Homo sapiens

Seq: Struc:					265 a.a. 109 a.a.

Key:

PfamA domain

Secondary structure

CATH domain



		Enzyme reactions

Enzyme class:

E.C.?

[IntEnz] [ExPASy] [KEGG] [BRENDA]

DOI no: 10.1107/S2053230X15013576	Acta Crystallogr F Struct Biol Commun 71:1169-1175 (2015)
PubMed id: 26323304

Structure of the N-terminal dimerization domain of CEACAM7.
D.A.Bonsor, D.Beckett, E.J.Sundberg.

ABSTRACT

CEACAM7 is a human cellular adhesion protein that is expressed on the surface of colon and rectum epithelial cells and is downregulated in colorectal cancers. It achieves cell adhesion through dimerization of the N-terminal IgV domain. The crystal structure of the N-terminal dimerization domain of CEACAM has been determined at 1.47 Å resolution. The overall fold of CEACAM7 is similar to those of CEACAM1 and CEACAM5; however, there are differences, the most notable of which is an insertion that causes the C'' strand to buckle, leading to the creation of a hydrogen bond in the dimerization interface. The Kdimerization for CEACAM7 determined by sedimentation equilibrium is tenfold tighter than that measured for CEACAM5. These findings suggest that the dimerization affinities of CEACAMs are modulated via sequence variation in the dimerization surface.