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Article

Increased N-glycosylation efficiency by generation of an aromatic sequon on N135 of antithrombin.

PloS one - 1 Jan 2014

Aguila Sonia, Martínez-Martínez Irene, Dichiara Gilda, Gutiérrez-Gallego Ricardo, Navarro-Fernández José, Vicente Vicente, Corral Javier

Abstract excerpt

The inefficient glycosylation of consensus sequence on N135 in antithrombin explains the two glycoforms of this key anticoagulant serpin found in plasma: α and β, with four and three N-glycans, respectively. The lack of this N-glycan increases the heparin affinity of the β-glycoform. Recent studies have demonstrated that an aromatic sequon (Phe-Y-Asn-X-Thr) in reverse β-turns enhances N-glycosylation efficiency...

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Identifiers

PMID: 25485983
DOI: 10.1371/journal.pone.0114454
PMCID: PMC4259341

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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