Effect of Site-Specific O-Glycosylation on the Structural Behavior of NOTCH1 Receptor Extracellular EGF-like Domains 11 and 10.
NMR spectroscopy
glycosylation
protein models
protein structure
synthetic glycopeptide
Journal
Chemistry (Weinheim an der Bergstrasse, Germany)
ISSN: 1521-3765
Titre abrégé: Chemistry
Pays: Germany
ID NLM: 9513783
Informations de publication
Date de publication:
25 Sep 2020
25 Sep 2020
Historique:
received:
01
06
2020
pubmed:
8
7
2020
medline:
20
2
2021
entrez:
8
7
2020
Statut:
ppublish
Résumé
Human NOTCH1 receptor contains 36 epidermal growth factor (EGF)-like repeating domains, in which O-glycosylation status of EGF12 domain regulates the interaction with Notch ligands. Our interest is focused on the effect of specific O-glycosylation states on the structural behavior of EGF11 and EGF10, because they appeared to affect molecular mechanism in receptor-ligand interactions by inducing some conformational alterations in these domains and/or the regions connecting two domains. To understand the structural impact of various O-glycosylation patterns on the pivotal EGF-like repeats 10, 11, and 12, we performed chemical synthesis and NMR studies of site-specifically O-glycosylated EGF11 and EGF10. Our strategy enabled us to synthesize four EGF11 and five EGF10 modules. The specific O-glycosylation states affected in vitro folding of EGF10 more than EGF11, while calcium ion had a larger effect on EGF11 folding. Comprehensive NMR studies shed light on the new type "sugar bridges" crosslinking Thr-O-GlcNAc in the consensus sequence C5-X-X-G-X-(T/S)-G-X-X-C6 and an amino acid in the hinge region between the domains, 445Thr-O-GlcNAc-IIe451 in domain 11 and 405Thr-O-GlcNAc-Gln411 in domain 10, respectively.
Identifiants
pubmed: 32632967
doi: 10.1002/chem.202002652
doi:
Substances chimiques
Ligands
0
NOTCH1 protein, human
0
Receptor, Notch1
0
Epidermal Growth Factor
62229-50-9
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
12363-12372Informations de copyright
© 2020 Wiley-VCH GmbH.
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