About: Structural basis of the dynamic human CEACAM1 monomer-dimer equilibrium

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An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Structural basis of the dynamic human CEACAM1 monomer-dimer equilibrium
Creator	Huang, Yu-Hwa Wagner, Gerhard Gandhi, Amit Blumberg, Richard Petsko, Gregory Bonsor, Daniel Kim, Walter Kondo, Kuchroo, Sun, Zhen-Yu Sundberg, Eric
Source	BioRxiv
abstract	Human (h) carcinoembryonic antigen-related cell adhesion molecule 1 (CEACAM1) function depends upon IgV-mediated homodimerization or heterodimerization with host ligands, including hCEACAM5 and hTIM-3, 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 monomer. These studies reveal the flexibility of the GFCC’ face and its important role in governing the formation of hCEACAM1 dimers and potentially heterodimers.
has issue date	2020-07-15(xsd:dateTime)
bibo:doi	10.1101/2020.07.14.199711
has license	biorxiv
sha1sum (hex)	ed24a34f9da92cf701031cf35c4c91092926fbb7
schema:url	https://doi.org/10.1101/2020.07.14.199711
resource representing a document's title	Structural basis of the dynamic human CEACAM1 monomer-dimer equilibrium
schema:publication	bioRxiv
resource representing a document's body	covid:ed24a34f9da92cf701031cf35c4c91092926fbb7#body_text
is schema:about of	named entity 'heterodimerization' named entity 'function' named entity 'homodimers' named entity 'angiogenesis' named entity 'pathogens' named entity 'CEACAM1' named entity 'dimer' named entity 'x-ray' named entity 'cross-correlation' named entity 'tyrosine' named entity 'CEACAM1' named entity 'fungi' named entity 'molecule' named entity 'electron density' named entity 'NMR' named entity 'dimer' named entity 'adhesins' named entity 'alternatively spliced' named entity 'low complexity' named entity 'NMR studies' named entity 'dimer' named entity 'crystal structure' named entity 'nitrogen' named entity 'carbohydrate' named entity 'monomer' named entity 'ligands' named entity 'amino acid residues' named entity 'dimers' named entity 'isoforms' named entity 'homodimerization' named entity 'alanine' named entity 'heterodimers' named entity 'single pass' named entity 'pulse train' named entity 'DSF' named entity '2C-D' named entity 'carbohydrate' named entity 'protein' named entity 'heterodimers' named entity 'PDB' named entity 'CPMG' named entity 'structural fold' named entity 'CPMG' named entity 'NMR' named entity 'crystal structure' named entity 'cis' named entity 'NMR' named entity 'monomer' named entity 'secondary structures' named entity 'monomers' named entity 'hexadentate' named entity 'site-directed' named entity 'NMR' named entity 'high affinity' named entity 'dimer' named entity 'ITIMs' named entity 'homodimers' named entity 'Q44' named entity 'monomer' named entity 'amino acid residues' named entity 'protein' named entity 'R43' named entity 'CEACAM1' named entity 'monoclonal antibody' named entity 'homodimer' named entity 'electron density' named entity 'site-directed mutagenesis' named entity 'NMR chemical shift' named entity 'N-terminal' named entity 'dynamic conformation' named entity 'homophilic' named entity 'PDB' named entity 'microbial' named entity 'single nucleotide polymorphisms'

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