Search results
Results from the WOW.Com Content Network
The different types of lipid-linked oligosaccharide (LLO) precursor produced in different organisms.. N-linked glycosylation is the attachment of an oligosaccharide, a carbohydrate consisting of several sugar molecules, sometimes also referred to as glycan, to a nitrogen atom (the amide nitrogen of an asparagine (Asn) residue of a protein), in a process called N-glycosylation, studied in ...
N-linked glycosylation is a very prevalent form of glycosylation and is important for the folding of many eukaryotic glycoproteins and for cell–cell and cell–extracellular matrix attachment. The N-linked glycosylation process occurs in eukaryotes in the lumen of the endoplasmic reticulum and widely in archaea, but very rarely in bacteria.
7841 57377 Ensembl n/a ENSMUSG00000030036 UniProt Q13724 Q80UM7 RefSeq (mRNA) NM_006302 NM_001146158 NM_020619 RefSeq (protein) NP_001139630 NP_006293 NP_065644 Location (UCSC) n/a Chr 6: 83.09 – 83.1 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Mannosyl-oligosaccharide glucosidase is an enzyme that in humans is encoded by the MOGS gene. Glucosidase I is the first enzyme in the ...
Structure of human galectin-9 in complex with N-acetyllactosamine dimer, clearly showing the two carbohydrate binding sites. Galectins are a class of proteins that bind specifically to β-galactoside sugars, such as N-acetyllactosamine (Galβ1-3GlcNAc or Galβ1-4GlcNAc), which can be bound to proteins by either N-linked or O-linked glycosylation.
The sugar Glc 3 Man 9 GlcNAc 2 (where Glc=Glucose, Man=Mannose, and GlcNAc=N-acetylglucosamine) is attached to an asparagine (Asn) residue in the sequence Asn-X-Ser or Asn-X-Thr where X is any amino acid except proline. This sequence is called a glycosylation sequon. The reaction catalyzed by OST is the central step in the N-linked ...
The mannose receptor is heavily glycosylated and its N-linked glycosylation sites are highly conserved between mice and humans, indicating an important role for this post-translational modification. The presence of sialic acid residues on N-linked glycans of the mannose receptor is important for its role in binding both sulphated and ...
N-Linked glycans derive their name from the fact that the glycan is attached to an asparagine (Asn, N) residue, and are amongst the most common linkages found in nature. Although the majority of N-linked glycans take the form GlcNAc-β-Asn [ 6 ] other less common structural linkages such as GlcNac-α-Asn [ 7 ] and Glc-Asn [ 8 ] have been observed.
[9] [12] It is known that the "A" form is glycosylated, whereas "B" is unglycosylated, and "C" is generated by cleavage of "B." [7] [9] In total, seven potential sites of N-linked glycosylation [7] has been observed in the center portion of the NRF3 protein. However, further details of the three forms' location, regulation, and function in each ...