Definition: N-linked glycosylation involves the attachment of glycans to the nitrogen atom of asparagine (Asn) residues in a specific sequence motif, typically denoted as Asn-X-Ser/Thr, where X can be any amino acid except proline (Pro) or aspartic acid (Asp)
Process
Location: This process begins in the endoplasmic reticulum (ER) and continues in the Golgi apparatus. The initial glycan structure is assembled as a lipid-linked oligosaccharide (LLO) before being transferred to the protein
Structure:
The glycan typically consists of a core structure that includes a
"tree" of 14 sugar residues, which is subsequently trimmed and
modified as the protein matures.
Function:
N-linked glycans play crucial roles in protein folding, stability, and cellular
recognition. They can also act as molecular signals for quality control
mechanisms during protein synthesis.
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