4Y89

Crystal structure of the N-terminal domain of CEACAM7

4Y89 の概要

• エントリーDOI: 10.2210/pdb4y89/pdb
• 関連するPDBエントリー: 4Y88 4Y8A 4Y8B
• 分子名称: Carcinoembryonic antigen-related cell adhesion molecule 7, CHLORIDE ION (3 entities in total)
• 機能のキーワード: cell adhesion
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 49929.71

構造登録者

Bonsor, D.A.,Sundberg, E.J. (登録日: 2015-02-16, 公開日: 2015-09-02, 最終更新日: 2023-09-27)

主引用文献

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

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: 26323304
DOI: 10.1107/S2053230X15013576

実験手法

X-RAY DIFFRACTION (1.47 Å)