Found 1 structure.
Displayed structure 1
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1. Compound ID: 27880
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a-Fucp-(1-4)-+
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b-Galp-(1-3)-b-D-GlcpNAc-(1-2)-a-D-Manp-(1-6)-+
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b-Fucp-(1-4)-+ | a-Fuc-(1-3)-+
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b-Galp-(1-3)-b-D-GlcpNAc-(1-2)-a-D-Manp-(1-3)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc-(1--/(->4) Asn-X-Ser/Thr (protein)/
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a-Xylp-(1-2)-+ |
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Structure type: oligomer
Aglycon: (->4) Asn-X-Ser/Thr (protein)
Compound class: N-glycan
Contained glycoepitopes: IEDB_114701,IEDB_115015,IEDB_123886,IEDB_123888,IEDB_130653,IEDB_130701,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_1391962,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_142078,IEDB_142489,IEDB_143794,IEDB_144562,IEDB_144983,IEDB_145669,IEDB_148493,IEDB_149135,IEDB_149556,IEDB_150092,IEDB_150899,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_153212,IEDB_167186,IEDB_174333,IEDB_190606,IEDB_423096,IEDB_461723,IEDB_490029,IEDB_548907,IEDB_983930,SB_137,SB_155,SB_165,SB_166,SB_187,SB_195,SB_197,SB_198,SB_29,SB_33,SB_44,SB_67,SB_7,SB_72,SB_73,SB_74,SB_85,SB_86,SB_88
The structure is contained in the following publication(s):
- Article ID: 10996
Rayon C, Lerouge P, Faye L "The protein N-glycosylation in plants" -
Journal of Experimental Botany 49(326) (1998) 1463–1472
In plants, most proteins of the extracellular compartment and the endomembrane system are glycosylated by N-linked oligosaccharides. The N-glycosylation of proteins has a great impact both on their physicochemical properties and on their biological functions. Over the last ten years, a number of laboratories have contributed considerably to the understanding of the structure, the biosynthesis and the function of plant N-linked glycans. In this review, data on this domain will be summarized and the recent results on the N-glycosylation of a vacuolar lectin, the bean phytohaemagglutinin (PHA) will also be included. This PHA, used as a model glycoprotein, was expressed in different plant systems and the N-glycosylation patterns of different recombinant PHA were compared. In addition to this study on plant-specific glycosylation, the same model glycoprotein was used to investigate whether or not N-glycosylation and N-glycan maturation is organ-specific in plants.
N-Linked oligosaccharide, biosynthesis and function, phytohaemagglutinin
Publication DOI: 10.1093/jxb/49.326.1463Journal NLM ID: 9882906Publisher: Oxford University Press
Correspondence: Faye L
Institutions: Laboratoire des Transports Intracellulaires, Université de Rouen, Mont Saint Aignan, France
Methods: NMR, column chromatography, PNGase A treatment, HPAED-PAD
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