By John S. Axford
ISBN-10: 0306477823
ISBN-13: 9780306477829
This ebook 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 approaches 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 sickness.
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Additional info for Glycobiology and Medicine
Sample text
The N-terminus of pilus subunits, which is disordered in chaperone:subunit complexes, harbors a conserved [3-strand motif similar to the chaperone G\ motif. , 1998). Pilus assembly was therefore suggested to proceed by a donor strand exchange (DSE) mechanism in which the chaperone G 1 donor strand is replaced by the N-terminus of a second subunit, thereby joining subunits into a fiber (Figure 3C). We recently obtained a structure for the Y. , 2003). The structure reveals two pilinlike subunits linked by DSC and provides the first direct evidence for the proposed DSE model for organelle assembly.
FimH-mediated binding requires terminal mannose residues. , 1999). The ellipsoid-shaped FimH lectin domain consists of eleven l3-strands in three l3-sheets arranged as a pseudo-twofold l3-barrel with a jelly roll-like topology. The tip of the domain has a deep pocket large enough to accommodate and completely bury a single mannose residue (Figure 4A). In the FimC:FimH structure, a carbohydrate analogue (C-HEGA, cyclohexylbutanoyl-N-hydroxyethyl-D-glucamide) occupied this pocket. , 2002) and of the lectin domain of FimH (1.
Knight imH PapG Figure 5. FimH (left) and PapG (right) lectin domains. Carbohydrates bound to the lectins in ball-and-stick. FimH FocH SfaH TLQR LRVRQ LKILK * * * ** FimH FocH SfaH FimH FocH SfaH * * FPTTSETPRVVYNSRTD LQQDTKPTEAYWQYG LQFDLQVTEAFYQYG G F ILRQTNNYNSDD -VYVNKFSTMGQEAGE ~K~~I~hJrrLYVNKFSTKGQEAGE * * *. ** * Figure 6. Sequence alignment of FimH, FocH, and SfaH, FimH. Identical residues shaded dark gray, homologous residues light gray. Residues in the C-HEGA pocket are indicated by "*,, below the sequences.
Glycobiology and Medicine by John S. Axford
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