Human CEACAM1 N-domain dimerization is independent from glycan modifications

Human CEACAM1 N-domain dimerization is independent from glycan modifications

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 cen...

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Bibliographic Details
Main Authors: Belcher Dufrisne, M. (Author), Columbus, L. (Author), Han, J. (Author), Kieber, M. (Author), Li, J. (Author), Moremen, K.W (Author), Prestegard, J.H (Author), Swope, N. (Author), Yang, J.-Y (Author)
Format: Article
Language:English
Published: Cell Press 2022
Subjects:
carcinoembryonic antigen-related cell adhesion molecule (CEACAM)
dimerization
double electron-electron EPR spectroscopy
electron paramagnetic (EPR) spectroscopy
glycosylation
X-ray crystallography
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