Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Although there is great interest in three-dimensional structures of glycoproteins and complex oligosaccharides, their structural determination have been hampered by inhomogeneous and incomplete glycosylation, poor expression, low tendency to crystallize, and severe chemical shift overlap. Using segmental labeling of the glycan and the protein component by in vitro glycosylation, we developed a novel method of NMR structural determination that overcomes some of these problems. Highly homogeneously glycosylated proteins in milligram amounts can be obtained. This allowed the determination of the structure of an N-linked glycoprotein from Campylobacter jejuni. The glycosylation acceptor site was found to be in a flexible loop. The presented methodology extends the observable NOE distance limit of oligosaccharides significantly over 4 A, resulting in a high number of distance restraints per glycosidic linkage. A well-defined glycan structure was obtained.
NMR structure determination of a segmentally labeled glycoprotein using in vitro glycosylation.,Slynko V, Schubert M, Numao S, Kowarik M, Aebi M, Allain FH J Am Chem Soc. 2009 Jan 28;131(3):1274-81. PMID:19154179[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Slynko V, Schubert M, Numao S, Kowarik M, Aebi M, Allain FH. NMR structure determination of a segmentally labeled glycoprotein using in vitro glycosylation. J Am Chem Soc. 2009 Jan 28;131(3):1274-81. PMID:19154179 doi:10.1021/ja808682v
