ArticleStructure (London, England : 1993)2022
Human CEACAM1 N-domain dimerization is independent from glycan modifications.
Article in Structure (London, England : 1993), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
9 citing papers in PubMed.
- A Multiscale Computational Architecture to Study Signaling Dynamics at Cell-Cell Interfaces.bioRxiv : the preprint server for biology · 2026Article
- The role of immune checkpoints in modulating cancer stem cells anti-tumor immune responses: implications and perspectives in cancer therapy.Journal of experimental & clinical cancer research : CR · 2025Review
- Structural aspects of CEACAM1 interactions.European journal of clinical investigation · 2024Review
- The role of CEACAMs in neutrophil function.European journal of clinical investigation · 2024Review
- Carcinoembryonic antigen-related cell adhesion molecule 1 in cancer: Blessing or curse?European journal of clinical investigation · 2024Review
- The role of carcinoembryonic antigen-related cell adhesion molecule 1 in cancer.Frontiers in immunology · 2023Review
- Glycan Conformation in the Heavily Glycosylated Protein, CEACAM1.ACS chemical biology · 2022Article
- Structural analysis of human CEACAM1 oligomerization.Communications biology · 2022Article
- Beyond structure: Deciphering site-specific dynamics in proteins from double histidine-based EPR measurements.Protein science : a publication of the Protein Society · 2022Article
Corrections and comments
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Authors and funding
9 authors.
Funding
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.