ArticleCommunications biology2021
Structural basis of the dynamic human CEACAM1 monomer-dimer equilibrium.
Article in Communications biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 15 citations in OpenAlex.
- Neutrophil CEACAMs and the Inflammatory Response toJournal of innate immunity · 2026Review
- Article
- Structural basis for immune cell binding ofProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structural aspects of CEACAM1 interactions.European journal of clinical investigation · 2024Review
- The role of CEACAMs in neutrophil function.European journal of clinical investigation · 2024Review
- CEACAM1 in vascular homeostasis and inflammation.European journal of clinical investigation · 2024Review
- High-dimensional mapping of human CEACAM1 expression on immune cells and association with melanoma drug resistance.Communications medicine · 2024Article
- Glycan Conformation in the Heavily Glycosylated Protein, CEACAM1.ACS chemical biology · 2022Article
- AssignSLP_GUI, a software tool exploiting AI for NMR resonance assignment of sparsely labeled proteins.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2022Article
- Structural analysis of human CEACAM1 oligomerization.Communications biology · 2022Article
- Human CEACAM1 N-domain dimerization is independent from glycan modifications.Structure (London, England : 1993) · 2022Article
- An investigation into the role of inherited CEACAM gene family variants and colorectal cancer risk.BMC research notes · 2022Article
- Multi-omics integration and interactomics reveals molecular networks and regulators of the beneficial effect of yoga and exercise.International journal of yogaArticle
Corrections and comments
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Authors and funding
11 authors at 4 institutions in 2 countries.
Funding
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.
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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.