Trends in Glycoscience and Glycotechnology
Online ISSN : 1883-2113
Print ISSN : 0915-7352
Volume 11 , Issue 57
Showing 1-4 articles out of 4 articles from the selected issue
  • Pauline M. Rudd, Mark R. Wormald, Raymond A. Dwek, [in Japanese], [in ...
    1999 Volume 11 Issue 57 Pages 1-21
    Published: January 02, 1999
    Released: January 05, 2010
    JOURNALS FREE ACCESS
    A full understanding of the implications of glycosylation for the structure and function of any glycoprotein can only be reached when the molecule is viewed in its entirety. Many glycoproteins are involved in the humoral and cellular immune systems and can, by virtue of their individual protein structures, influence the processing of their sugars. The sugars provide a range of functions for the proteins to which they are attached. These include stabilising the protein structure, modifying the activity of effector functions, orienting the protein on the cell surface, shielding the protein from proteases and providing specific epitopes for recognition events both in the glycoprotein folding process and on fully folded proteins. NMR solution and X-ray crystallography studies of glycoproteins do not normally yield detailed information about the sugars. In this review we discuss a range of molecules which operate in the immune system and in which protein structural data have been complemented by data from glycan analyses and the dimensions of the sugars taken from the Glycobiology Institute's oligosaccharide structural data base. In this way it has been possible to obtain a more complete view of each glycoprotein and of the proposed functions of the sugars. The glycoproteins include the immunoglobulins IgG, IgA and IgM which are involved in the humoral immune response. IgG and IgM activate the complement system which is controlled by a number of inhibitors, including CD59 and decay accelerating factor (DAF, CD55) which we also discuss. Examples of proteins involved in the cellular immune response include the cell adhesion molecules CD2 and CD48 which mediate the precise alignment of the cell surfaces of cytolytic T-lymphocytes carrying the T-cell receptor (TCR) complex with those of target cells carrying HLA class 1 molecules loaded with peptide.
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  • Junji Sugiyama, Tomoya Imai
    1999 Volume 11 Issue 57 Pages 23-31
    Published: January 02, 1999
    Released: January 05, 2010
    JOURNALS FREE ACCESS
    Native cellulose is one of the best studied natural polymers. Cellulose is synthesized by the coordinated action of enzymatic polymerization coupled with instant crystallization into nascent cellulose microfibrils. This mechanism allows the generation of highly extended chains that can crystallize into microfibrils including two distinct crystalline moieties; cellulose Iα and Iβ. The microfibrils are then assembled to form higher order structures such as layers, cell walls, fibers and tissues. Structural analyses of cellulose have been performed to determine both its primary structure and higher order structures as these markedly influence the function and properties of native cellulose. Here, we report recent advances in our knowledge regarding the structure of native cellulose at several different levels.
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  • Naoya Kojma
    1999 Volume 11 Issue 57 Pages 33-34
    Published: January 02, 1999
    Released: January 05, 2010
    JOURNALS FREE ACCESS
    Download PDF (367K)
  • Naoya Kojma
    1999 Volume 11 Issue 57 Pages 35-36
    Published: January 02, 1999
    Released: January 05, 2010
    JOURNALS FREE ACCESS
    Download PDF (418K)
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