scholarly journals Structural Basis for Recognition of High Mannose Type Glycoproteins by Mammalian Transport Lectin VIP36

2007 ◽  
Vol 282 (38) ◽  
pp. 28246-28255 ◽  
Author(s):  
Tadashi Satoh ◽  
Nathan P. Cowieson ◽  
Wataru Hakamata ◽  
Hiroko Ideo ◽  
Keiko Fukushima ◽  
...  
Keyword(s):  
Secretory Pathway ◽  
Structural Basis ◽  
Carbohydrate Binding ◽  
Carbohydrate Recognition Domain ◽  
Complex Structures ◽  
Carbohydrate Recognition ◽  
Specific Manner ◽  
Stalk Domain ◽  
High Mannose ◽  
Carbohydrate Binding Site

VIP36 functions as a transport lectin for trafficking certain high mannose type glycoproteins in the secretory pathway. Here we report the crystal structure of VIP36 exoplasmic/luminal domain comprising a carbohydrate recognition domain and a stalk domain. The structures of VIP36 in complex with Ca2+ and mannosyl ligands are also described. The carbohydrate recognition domain is composed of a 17-stranded antiparallel β-sandwich and binds one Ca2+ adjoining the carbohydrate-binding site. The structure reveals that a coordinated Ca2+ ion orients the side chains of Asp131, Asn166, and His190 for carbohydrate binding. This result explains the Ca2+-dependent carbohydrate binding of this protein. The Man-α-1,2-Man-α-1,2-Man, which corresponds to the D1 arm of high mannose type glycan, is recognized by eight residues through extensive hydrogen bonds. The complex structures reveal the structural basis for high mannose type glycoprotein recognition by VIP36 in a Ca2+-dependent and D1 arm-specific manner.

scholarly journals A bivalent glycopeptide to target two putative carbohydrate binding sites on FimH

2010 ◽  
Vol 6 ◽  
pp. 801-809 ◽  
Author(s):  
Thisbe K Lindhorst ◽  
Kathrin Bruegge ◽  
Andreas Fuchs ◽  
Oliver Sperling
Keyword(s):  
Binding Site ◽  
Binding Sites ◽  
Carbohydrate Binding ◽  
Carbohydrate Recognition Domain ◽  
Carbohydrate Recognition ◽  
Binding Studies ◽  
Bivalent Ligand ◽  
X Ray ◽  
Carbohydrate Binding Site

FimH is a mannose-specific bacterial lectin found on type 1 fimbriae with a monovalent carbohydrate recognition domain (CRD) that is known from X-ray studies. However, binding studies with multivalent ligands have suggested an additional carbohydrate-binding site on this protein. In order to prove this hypothesis, a bivalent glycopeptide ligand with the capacity to bridge two putative carbohydrate binding sites on FimH was designed and synthesized. Anti-adhesion assays with the new bivalent ligand and type 1-fimbriated bacteria have revealed, that verification of the number of carbohydrate binding sites on FimH with a tailor-made bivalent glycopeptide requires further investigation to be conclusive.

scholarly journals The carbohydrate-recognition domain of Dectin-2 is a C-type lectin with specificity for high mannose

Glycobiology ◽  
2006 ◽  
Vol 16 (5) ◽  
pp. 422-430 ◽  
Author(s):  
Eamon P. McGreal ◽  
Marcela Rosas ◽  
Gordon D. Brown ◽  
Susanne Zamze ◽  
Simon Y.C. Wong ◽  
...  
Keyword(s):  
Carbohydrate Recognition Domain ◽  
Carbohydrate Recognition ◽  
High Mannose

scholarly journals Structural basis for the unusual carbohydrate-binding specificity of jacalin towards galactose and mannose

2002 ◽  
Vol 364 (1) ◽  
pp. 173-180 ◽  
Author(s):  
Yves BOURNE ◽  
Corinne Houlès ASTOUL ◽  
Véronique ZAMBONI ◽  
Willy J. PEUMANS ◽  
Laurence MENU-BOUAOUICHE ◽  
...  
Keyword(s):  
Surface Plasmon Resonance ◽  
T Antigen ◽  
Structural Basis ◽  
Carbohydrate Binding ◽  
X Ray ◽  
Acetylneuraminic Acid ◽  
Large Size ◽  
Biochemical Analyses ◽  
Carbohydrate Binding Site

Evidence is presented that the specificity of jacalin, the seed lectin from jack fruit (Artocarpus integrifolia), is not directed exclusively against the T-antigen disaccharide Galβ1,3GalNAc, lactose and galactose, but also against mannose and oligomannosides. Biochemical analyses based on surface-plasmon-resonance measurements, combined with the X-ray-crystallographic determination of the structure of a jacalin—α-methyl-mannose complex at 2Å resolution, demonstrated clearly that jacalin is fully capable of binding mannose. Besides mannose, jacalin also interacts readily with glucose, N-acetylneuraminic acid and N-acetylmuramic acid. Structural analyses demonstrated that the relatively large size of the carbohydrate-binding site enables jacalin to accommodate monosaccharides with different hydroxyl conformations and provided unambiguous evidence that the β-prism structure of jacalin is a sufficiently flexible structural scaffold to confer different carbohydrate-binding specificities to a single lectin.

Genomic analysis of C-type lectins

2002 ◽  
Vol 69 ◽  
pp. 59-72 ◽  
Author(s):  
Kurt Drickamer ◽  
Andrew J. Fadden
Keyword(s):  
Biological Effects ◽  
Cell Signalling ◽  
Genomic Analysis ◽  
Binding Activity ◽  
Immunoglobulin Superfamily ◽  
Carbohydrate Binding ◽  
Carbohydrate Recognition ◽  
Calcium Dependent ◽  
Binding Domains ◽  
Carbohydrate Recognition Domains

Many biological effects of complex carbohydrates are mediated by lectins that contain discrete carbohydrate-recognition domains. At least seven structurally distinct families of carbohydrate-recognition domains are found in lectins that are involved in intracellular trafficking, cell adhesion, cell–cell signalling, glycoprotein turnover and innate immunity. Genome-wide analysis of potential carbohydrate-binding domains is now possible. Two classes of intracellular lectins involved in glycoprotein trafficking are present in yeast, model invertebrates and vertebrates, and two other classes are present in vertebrates only. At the cell surface, calcium-dependent (C-type) lectins and galectins are found in model invertebrates and vertebrates, but not in yeast; immunoglobulin superfamily (I-type) lectins are only found in vertebrates. The evolutionary appearance of different classes of sugar-binding protein modules parallels a development towards more complex oligosaccharides that provide increased opportunities for specific recognition phenomena. An overall picture of the lectins present in humans can now be proposed. Based on our knowledge of the structures of several of the C-type carbohydrate-recognition domains, it is possible to suggest ligand-binding activity that may be associated with novel C-type lectin-like domains identified in a systematic screen of the human genome. Further analysis of the sequences of proteins containing these domains can be used as a basis for proposing potential biological functions.

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