6XNT

Crystal structure of I91A mutant of human CEACAM1

6XNT の概要

• エントリーDOI: 10.2210/pdb6xnt/pdb
• 関連するPDBエントリー: 6XNO
• 分子名称: Carcinoembryonic antigen-related cell adhesion molecule 1, octyl beta-D-glucopyranoside (3 entities in total)
• 機能のキーワード: ceacam1, immune system
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 24298.92

構造登録者

Gandhi, A.K.,Kim, W.M.,Sun, Z.-Y.,Huang, Y.H.,Bonsor, D.,Petsko, G.A.,Kuchroo, V.,Blumberg, R.S. (登録日: 2020-07-04, 公開日: 2021-03-24, 最終更新日: 2023-10-18)

主引用文献

Gandhi, A.K.,Sun, Z.J.,Kim, W.M.,Huang, Y.H.,Kondo, Y.,Bonsor, D.A.,Sundberg, E.J.,Wagner, G.,Kuchroo, V.K.,Petsko, G.A.,Blumberg, R.S.
Structural basis of the dynamic human CEACAM1 monomer-dimer equilibrium.
Commun Biol, 4:360-360, 2021

PubMed Abstract: Human (h) carcinoembryonic antigen-related cell adhesion molecule 1 (CEACAM1) function depends upon IgV-mediated homodimerization or heterodimerization with host ligands, including hCEACAM5, hTIM-3, PD-1, and a variety of microbial pathogens. However, there is little structural information available on how hCEACAM1 transitions between monomeric and dimeric states which in the latter case is critical for initiating hCEACAM1 activities. We therefore mutated residues within the hCEACAM1 IgV GFCC' face including V39, I91, N97, and E99 and examined hCEACAM1 IgV monomer-homodimer exchange using differential scanning fluorimetry, multi-angle light scattering, X-ray crystallography and/or nuclear magnetic resonance. From these studies, we describe hCEACAM1 homodimeric, monomeric and transition states at atomic resolution and its conformational behavior in solution through NMR assignment of the wildtype (WT) hCEACAM1 IgV dimer and N97A mutant monomer. These studies reveal the flexibility of the GFCC' face and its important role in governing the formation of hCEACAM1 dimers and selective heterodimers.

PubMed: 33742094
DOI: 10.1038/s42003-021-01871-2

実験手法

X-RAY DIFFRACTION (3.1 Å)