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Structure paper

TitleHuman CEACAM1 N-domain dimerization is independent from glycan modifications.
Journal, issue, pagesStructure, Vol. 30, Page 658-670.e5, Year 2022
Publish dateMay 14, 2021 (structure data deposition date)
AuthorsBelcher Dufrisne, M. / Swope, N. / Kieber, M. / Yang, J.Y. / Han, J. / Li, J. / Moremen, K.W. / Prestegard, J.H. / Columbus, L.
External linksStructure / PubMed:35219398
MethodsX-ray diffraction
Resolution1.7 Å
Structure data

PDB-7mu8:
Structure of the minimally glycosylated human CEACAM1 N-terminal domain
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-GOL:
GLYCEROL

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsCELL ADHESION / CEACAM1 / dimer / immunoglobulin fold / glycosylated

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