Structural Model and trans-Interaction of the Entire Ectodomain of the Olfactory Cell Adhesion Molecule
Copyright policy )Structural Model and trans-Interaction of the Entire Ectodomain of the Olfactory Cell Adhesion Molecule
The ectodomain of olfactory cell adhesion molecule (OCAM/NCAM2/RNCAM) consists of five immunoglobulin (Ig) domains (IgI-V), followed by two fibronectin-type 3 (Fn3) domains (Fn3I-II). A complete structural model of the entire ectodomain of human OCAM has been assembled from crystal structures of six recombinant proteins corresponding to different regions of the ectodomain. The model is the longest experimentally based composite structural model of an entire IgCAM ectodomain. It displays an essentially linear arrangement of IgI-V, followed by bends between IgV and Fn3I and between Fn3I and Fn3II. Proteins containing IgI-IgII domains formed stable homodimers in solution and in crystals. Dimerization could be disrupted in vitro by mutations in the dimer interface region. In conjunction with the bent ectodomain conformation, which can position IgI-V parallel with the cell surface, the IgI-IgII dimerization enables OCAM-mediated trans-interactions with an intercellular distance of about 20 nm, which is consistent with that observed in synapses.
- University of Copenhagen Denmark
- ENKAM PHARMACEUTICALS A/S Denmark
- HAGEDORN RESEARCH INSTITUTE
- University of Copenhagen Denmark
- University of copenhaguen Denmark
Faculty of Health and Medical Sciences, /dk/atira/pure/core/keywords/TheFacultyOfHealthScience, Molecular Sequence Data, Gene Expression, Immunoglobulins, Molecular Dynamics Simulation, Crystallography, X-Ray, Pichia, Structural Biology, Humans, Protein Interaction Domains and Motifs, Amino Acid Sequence, Molecular Biology, Neural Cell Adhesion Molecules, Binding Sites, Cell Membrane, Recombinant Proteins, Fibronectins, Models, Structural, Synapses, Dimerization, Protein Binding
Faculty of Health and Medical Sciences, /dk/atira/pure/core/keywords/TheFacultyOfHealthScience, Molecular Sequence Data, Gene Expression, Immunoglobulins, Molecular Dynamics Simulation, Crystallography, X-Ray, Pichia, Structural Biology, Humans, Protein Interaction Domains and Motifs, Amino Acid Sequence, Molecular Biology, Neural Cell Adhesion Molecules, Binding Sites, Cell Membrane, Recombinant Proteins, Fibronectins, Models, Structural, Synapses, Dimerization, Protein Binding
citations This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).26 popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.Top 10% influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).Average impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.Top 10%
Citations provided by BIP!Popularity provided by BIP!