Journal
BIOORGANIC & MEDICINAL CHEMISTRY
Volume 27, Issue 13, Pages 2822-2831Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.bmc.2019.05.008
Keywords
O-mannose type glycans; Dystroglycan; Microarray; Conformational change; POMGnT1
Funding
- Innovation COE program for future Drug Discovery and Medical Care from the MEXT Japan
- JSPS [23350074, 17K05920]
- Hoansha Foundation
- Japan Keirin and Autorace Association [2018M-100]
- Grants-in-Aid for Scientific Research [23350074, 17K05920] Funding Source: KAKEN
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Structural and functional effects of core M1 type glycan modification catalyzed by protein O-linked mannose beta 1,2-N-acetylglucosaminyltransferase 1 (POMGnT1) were investigated using a core M1 glycoform focused library of an alpha-dystroglycan fragment, (372)TRGAIIQTPTLGPIQPTRV(390). Evanescent-field fluorescence-assisted microarray system illuminated the specific binding pattern of plant lectins that can discriminate the glycan structure of core M1 glycan of the library. The comparative NMR analysis of synthetic glycopeptide having different length of the O-mannosylated glycans revealed a conformational change of the peptide backbone along with core M1 disaccharide formation. No long-range NOE signals of glycan-amino acid nor inter amino acid indicate the conformational change is induced by steric hindrance of core M1, the sole 1,2-O-modified form among protein binding sugar residue found in mammals.
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