![]() Its highest expression is in specific adult human brain regions such as the cerebral cortex, a region involved in sensory-motor function, cognition and working memory the hippocampus, responsible for long-term memory and the encoding and retrieval of multi-sensory information the amygdala, implicated in the stress response as well as the thalamus, with a more constant and basal level of expression across the remainder of the brain. It is targeted to the plasma membrane of neurons, but it is possible that a smaller quantities of the protein may be found in other intracellular compartments. LINGO-1 mRNA is expressed in an almost exclusive manner in the central nervous system during both embryonic and postnatal stages. It can be found in the brain and in neurons and oligodendrocytes. LINGO-1 is expressed almost exclusively in the central nervous system (CNS). Blue is for the actions of the protein in the nervous system whereas purple represents the secretory function of LINGO-1 in the pancreas. Tissue distribution Graphical summary of the expression of the LINGO-1 gene in humans. LINGO-1 contains several N-glycosylation sites that could have a negative effect on its capacity to self-interact with cis or trans, with other partners, or gangliosides. LINGO-1 is an homotetramer which forms a ternary complex with RTN4R/ NGFR and RTN4R/ TNFRSF19. The Nogo receptor complex is formed when Nogo-66 binds to its receptor. LINGO-1 is a co-receptor that interacts with the ligand-binding Nogo-66 receptor (NogoR) in the Nogo receptor signaling complex. It contains a canonical Epidermal Growth Factor Receptor (EGFR)-like tyrosine phosphorylation site on the 591 residue that is critical for intracellular signals. The intracellular part of the protein is formed by the transmembrane region and a cytoplasmic tail of 38 residues. ![]() The structure, together with biophysical analysis of LINGO-1 properties have revealed that the protein's LRR-Ig composite fold of the protein can drive it to associate with itself in a circular ring-like form, creating a closed and stable tetramer in solution and in crystal. The C-terminal LRR domain is essential for the protein's function with its screening for proteins that interact with this domain. ![]() The extracellular domain consists of the signal sequence, 11 LRR motifs comprised between an N-terminal and C-terminal capping domains, and the Immunoglobulin-like ( IgC2) domain. Since the tetramer has a very large surface area into the cell membrane, it is thought that this may serve as an efficient and stable binding platform, facilitating the interaction with NgR, p75, TROY complex. The LINGO-1 structure has been shown to be highly stable both in its crystal form and in solution, thanks to its leucine-rich repeat Ig-composite fold. As a transmembrane protein, it can mostly be found on the cell membrane. It contains a signal sequence of 34 residues, followed by a LRR ( leucine-rich repeat) domain, an Ig (immunoglobulin-like) domain, a stalk domain, a transmembrane region and a short cytoplasmic tail. The human LINGO-1 is a single-pass type 1 transmembrane protein of 614 amino acids. The different domains are signaled according to their chemical characteristics and their aminoacids are identified. Structure Aminoacidic sequence of the human LINGO-1 protein. It has been suggested that LINGO-1 antagonists such as BIIB033 could significantly improve and regulate survival after neural injury caused by the protein. LINGO-1 is a functional component of the Nogo (neurite outgrowth inhibitor) receptor also known as the reticulon 4 receptor. It belongs to the family of leucine-rich repeat proteins which are known for playing key roles in the biology of the central nervous system. Leucine rich repeat and Immunoglobin-like domain-containing protein 1 also known as LINGO-1 is a protein which is encoded by the LINGO1 gene in humans.
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