Increased N-glycosylation efficiency by generation of an aromatic sequon on N135 of antithrombin.
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...
| Published in: | PLoS ONE |
|---|---|
| Main Authors: | , , , , , , |
| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2014-01-01
|
| Online Access: | http://europepmc.org/articles/PMC4259341?pdf=render |
