Glycoproteins structure determination

Dell A. and Morris H.R. (2001), Glycoprotein structure determination by mass spectrometry, Science 291, 2351-2356. 

A. Dell, H.R. Morris, Glycoprotein structure determination mass spectrometry, Science 2001, 291, 2351-2356. 

Anne Dell, Howard R. Morris, Glycoprotein Structure Determination by Mass Spectrometry, Science, 291 (2001), 2351-2356. 

Yates CR, Chang C, Kearbey JD, Yasuda K, Schuetz EG, Miller DD, et al. Structural determinants of P-glycoprotein-mediated transport of glucocorticoids. Pharm Res 2003 20 1794-803. 

The final chapter, by Hounsell (London), also relates to an important aspect of glycoprotein structure, namely the structures and shapes, as determined by physicochemical methods, of oligosaccharide determinants of glycoproteins that are antigens and targets for binding of adhesion molecules. 

Fig. 5. Schematic diagram summarizing the available structural information on the Halobacterium cell envelope from X-ray studies of the envelopes (Blaurock el al., 1976), from the primary structure of the surface glycoprotein (Lechner and Sumper, 1987), and from the three-dimensional structure described by Kessel el al. (1988). The three-dimensional structure determined by electron microscopy depicts only the upper dome-shaped region of the structure, which is separated from the cell membrane by the spacer elements. As indicated by the crystallographic symbols, the section runs from sixfold to sixfold axis via the twofold axis. From Kessel et al., (1988), with permission.

The presence of the glycan (light blue) on ribonuclease B reduces the amide proton/deuteiium exchange rates compared with ribonuclease A for extensive regions of the peptide backbone (shown in red) both local to and remote from the glycosylation site [47]. The glycoprotein structure is based on the crystal structure of ribonuclease B [53] and one of the structures of MangGlcNAc2 determined by NMR and molecular dynamics. (Reprinted from [44] with permission from Elsevier), [54]... 

The Grijfonia simplicifolia IV (GS IV) lectin is a heterodimer composed of subunits of Mr = 27000 and 29000 Da [223]. The lectin, a glycoprotein, reacted most strongly with H and Le blood group substance [223,224]. GS IV has been crystallized and its X-ray structure determined [51]. 

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