7MU8

Structure of the minimally glycosylated human CEACAM1 N-terminal domain

7MU8 の概要

• エントリーDOI: 10.2210/pdb7mu8/pdb
• 分子名称: Carcinoembryonic antigen-related cell adhesion molecule 1, 2-acetamido-2-deoxy-beta-D-glucopyranose, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: ceacam1, dimer, immunoglobulin fold, glycosylated, cell adhesion
• 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: 25478.97

構造登録者

Belcher Dufrisne, M.,Swope, N.,Kieber, M.,Yang, J.Y.,Han, J.,Li, J.,Moremen, K.W.,Prestegard, J.H.,Columbus, L. (登録日: 2021-05-14, 公開日: 2022-02-09, 最終更新日: 2024-10-30)

主引用文献

Belcher Dufrisne, M.,Swope, N.,Kieber, M.,Yang, J.Y.,Han, J.,Li, J.,Moremen, K.W.,Prestegard, J.H.,Columbus, L.
Human CEACAM1 N-domain dimerization is independent from glycan modifications.
Structure, 30:658-670.e5, 2022

PubMed Abstract: Carcinoembryonic cellular adhesion molecules (CEACAMs) serve diverse roles in cell signaling, proliferation, and survival and are made up of one or several immunoglobulin (Ig)-like ectodomains glycosylated in vivo. The physiological oligomeric state and how it contributes to protein function are central to understanding CEACAMs. Two putative dimer conformations involving different CEACAM1 N-terminal Ig-like domain (CCM1) protein faces (ABED and GFCC'C″) were identified from crystal structures. GFCC'C″ was identified as the dominant CCM1 solution dimer, but ambiguity regarding the effect of glycosylation on dimer formation calls its physiological relevance into question. We present the first crystal structure of minimally glycosylated CCM1 in the GFCC'C″ dimer conformation and characterization in solution by continuous-wave and double electron-electron resonance electron paramagnetic resonance spectroscopy. Our results suggest the GFCC'C″ dimer is dominant in solution with different levels of glycosylation, and structural conservation and co-evolved residues support that the GFCC'C″ dimer is conserved across CEACAMs.

PubMed: 35219398
DOI: 10.1016/j.str.2022.02.003

実験手法

X-RAY DIFFRACTION (1.7 Å)