Download Glycobiology and Medicine by John S. Axford PDF

By John S. Axford

This e-book comprises the lawsuits of the 6th Jenner Glycobiology and medication Symposium, held 14-17 September, 2002, in Seillac, France.

This publication highlights the most recent advancements in glycoimmunology, together with glycosylation-dependent bacterial and viral infections, lectin and proteoglycan-dependent interactions in leukocyte homing strategies to lymphoid tissues and infected tissues, congenital defects in glycosylation of glycoproteins and glycolipids, and the function of carbohydrates in tumour improvement and neuropathology, together with Creutzfeldt-Jakob affliction.

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PapK and the pilin-domain of FimH have similar Ig-like folds, except that the final (G) strand ofthe fold is missing. The missing strand leaves a large cleft between the pi1in A and F strands, lined by hydrophobic residues from the core of the pilin. The chaperones bind the subunits by inserting their G 1 [3-strand into this cleft in a process called donor strand complementation (DSC) (Figure 3B). The G\ strand is lodged between the pilin A and F strands with extensive main-chain-to-main-chain hydrogen bonding between the pilin and the chaperone.

29:777-807. , 3 STRUCTURAL BASIS FOR BACTERIAL ADHESION IN THE URINARY TRACT Jenny Berglund and Stefan D. Knight Department of Molecular Biosciences/Structural Biology Uppsala Biomedical Center Swedish University of Agricultural Sciences Box 590, SE-753 24 Uppsala, Sweden 1. INTRODUCTION Most bacterial infections occur in the respiratory, gastrointestinal, or urinary tract. These spaces offer attractive advantages for bacteria in the form of nutrient availability, and are readily accessible from the outside world.

Berglund and S. D. Knight 38 A c Donor ~t ran d 'ccptor clen lapcronc Pilln donuun As embl Ubuillt Pl lin domain Figure 3. (A) Ribbon diagram of FimC:FimH complex. FimC chaperone in light gray, FimH in dark gray, G 1 donor strand of FimC colored black. (B) FimC G 1 donor-strand in FimH acceptor cleft. Donated hydrophobic residues are indicated. (C) Schematic of DSC. Pilin domains can be thought of as rearranged Ig domains where the C-terrninal G strand has been moved to the N-terrninus, creating a hydrophobic acceptor cleft on the surface of the Ig barrel and an N-terrninal donor strand.

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