The CEACAM1 N-terminal Ig domain mediates cis- and trans-binding and is essential for allosteric rearrangements of CEACAM1 microclusters
AUTOR(ES)
Klaile, Esther
FONTE
The Rockefeller University Press
RESUMO
Structural analyses reveal that oligomerization between cell adhesion molecules in the same membrane is influenced by their interactions across opposing membranes (see also in this issue the accompanying paper by Müller et al.).
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2779236Documentos Relacionados
- N-Terminal Domain of the Murine Coronavirus Receptor CEACAM1 Is Responsible for Fusogenic Activation and Conformational Changes of the Spike Protein
- The N-Terminal Domain of the Murine Coronavirus Spike Glycoprotein Determines the CEACAM1 Receptor Specificity of the Virus Strain
- The N-terminal 33 amino acid domain of Siva-1 is sufficient for nuclear localization
- The RAG1 N-terminal domain is an E3 ubiquitin ligase
- N-Terminal Domain–Mediated Homodimerization Is Required for Photoreceptor Activity of Arabidopsis CRYPTOCHROME 1