Found 1 structure.
Displayed structure 1
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1. Compound ID: 28537
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?%a-D-Manp-(1-2)-?%a-D-Manp-(1-2)-a-D-Manp-(1-3)-+
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?%a-D-Manp-(1-2)-a-D-Manp-(1-6)-+ |
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?%a-D-Manp-(1-2)-a-D-Manp-(1-3)-a-D-Manp-(1-6)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc-(1--/(->4) Asn-X-Ser/Thr (PHA)/ |
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Structure type: oligomer
Aglycon: (->4) Asn-X-Ser/Thr (PHA)
Compound class: N-glycan
Contained glycoepitopes: IEDB_123886,IEDB_130701,IEDB_135813,IEDB_136104,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_140942,IEDB_141793,IEDB_141807,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141831,IEDB_143632,IEDB_144983,IEDB_151079,IEDB_151531,IEDB_152206,IEDB_153212,IEDB_153220,IEDB_164046,IEDB_164174,IEDB_187201,IEDB_187238,IEDB_187239,IEDB_187240,IEDB_429156,IEDB_540671,IEDB_548907,IEDB_857734,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_33,SB_44,SB_53,SB_67,SB_72,SB_73,SB_74,SB_77,SB_85
The structure is contained in the following publication(s):
- Article ID: 11302
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, CC, PNGase A treatment, HPAED-PAD
- Article ID: 11303
Lerouge P, Rayon C, Gomord V, Faye L "N-glycoprotein biosynthesis in plants: recent developments and future trends" -
Plant Molecular Biology 38(1-2) (1998) 31-48
N-glycosylation is a major modification of proteins in plant cells. This process starts in the endoplasmic reticulum by the co-translational transfer of a precursor oligosaccharide to specific asparagine residues of the nascent polypeptide chain. Processing of this oligosaccharide into high-mannose-type, paucimannosidic-type, hybrid-type or complex-type N-glycans occurs in the secretory pathway as the glycoprotein moves from the endoplasmic reticulum to its final destination. At the end of their maturation, some plant N-glycans have typical structures that differ from those found in their mammalian counterpart by the absence of sialic acid and the presence of beta(1,2)-xylose and alpha(1,3)-fucose residues. Glycosidases and glycosyltransferases that respectively catalyse the stepwise trimming and addition of sugar residues are generally considered as working in a co-ordinated and highly ordered fashion to form mature N-glycans. On the basis of this assembly line concept, fast progress is currently made by using N-linked glycan structures as milestones of the intracellular transport of proteins along the plant secretory pathway. Further developments of this approach will need to more precisely define the topological distribution of glycosyltransferases within a plant Golgi stack. In contrast with their acknowledged role in the targeting of lysosomal hydrolases in mammalian cells, N-glycans have no specific function in the transport of glycoproteins into the plant vacuole. However, the presence of N-glycans, regardless of their structures, is necessary for an efficient secretion of plant glycoproteins. In the biotechnology field, transgenic plants are rapidly emerging as an important system for the production of recombinant glycoproteins intended for therapeutic purposes, which is a strong motivation to speed up research in plant glycobiology. In this regard, the potential and limits of plant cells as a factory for the production of mammalian glycoproteins will be illustrated.
plant, Recombinant Proteins, Arabidopsis thaliana, N-glycosylation
NCBI PubMed ID: 9738959Publication DOI: 10.1023/A:1006012005654Journal NLM ID: 9106343Publisher: Dordrecht: Kluwer Academic
Correspondence: Faye L
Institutions: Laboratoire des Transports Intracellulaires, Université de Rouen, Mont Saint Aignan, France
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