4Y89
Crystal structure of the N-terminal domain of CEACAM7
Summary for 4Y89
| Entry DOI | 10.2210/pdb4y89/pdb |
| Related | 4Y88 4Y8A 4Y8B |
| Descriptor | Carcinoembryonic antigen-related cell adhesion molecule 7, CHLORIDE ION (3 entities in total) |
| Functional Keywords | cell adhesion |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 4 |
| Total formula weight | 49929.71 |
| Authors | Bonsor, D.A.,Sundberg, E.J. (deposition date: 2015-02-16, release date: 2015-09-02, Last modification date: 2023-09-27) |
| Primary citation | Bonsor, D.A.,Beckett, D.,Sundberg, E.J. Structure of the N-terminal dimerization domain of CEACAM7. Acta Crystallogr.,Sect.F, 71:1169-1175, 2015 Cited by PubMed 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. PubMed: 26323304DOI: 10.1107/S2053230X15013576 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.47 Å) |
Structure validation
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