Structure of a C-type mannose-binding protein complexed with an oligosaccharide

Weis, William I.; Drickamer, Kurt; Hendrickson, Wayne A.

doi:10.1038/360127a0

Cited by 899 publications

(708 citation statements)

References 47 publications

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“…The docking of -glucose into the SP-D receptor site was essentially as expected based on the known crystallographic structures of MBP-A complexed with an oligosaccharide (12) and MBP-C complexed with various monosaccharides (11). The structures shown in Figure 2 closely resemble the MBP structures where the predominant binding interactions are between the protein and vicinal, equatorial OH groups at the 3 and 4 positions on the sugar ring.…”

Section: Discussionsupporting

confidence: 62%

“…Several structures of MBP complexed with carbohydrate ligands have been reported (11,12). On the basis of these …”

Section: Resultsmentioning

confidence: 99%

“…This has led previous investigators to speculate that interactions similar to those shown in Figure 3 may not occur for MBP (12). However, there are no steric factors precluding this binding arrangement, and as will be discussed below, we (11,12). Other notes as in Figure 1.…”

Section: Docking Of Glucose Into Sp-dmentioning

confidence: 90%

“…However, due to ring twist the 3-and 4-OH groups cannot be superimposed on the 2-and 3-OH groups. This has been used to explain why MBP binds glucose and mannose but not galactose (12). On the basis of previous structural analysis, it was not considered that the lectin could bind a ligand through interactions equivalent to those shown in Figure 3.…”

Section: Discussionmentioning

confidence: 99%

“…These studies have shown that MBP specifically recognizes vicinal, equatorial OH groups on monosaccharides equivalent to those present at the 3 and 4 positions of sugars such as mannose and glucose (13). It appears that MBP recognizes similar OH groups present on the nonreducing terminal carbohydrate residues of polysaccharides (12). Given the sequence and structural similarities between the CRDs from SP-D and MBP, mutagenesis data (14,15), and studies using various sugars as competitive inhibitors of carbohydrate recognition (7,10), it seems reasonable to conclude that SP-D recognizes carbohydrates by a mechanism similar to that of MBP.…”

Section: Sp-d Binds Many Microorganisms In Vitromentioning

confidence: 96%

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Polysaccharide Recognition by Surfactant Protein D: Novel Interactions of a C-Type Lectin with Nonterminal Glucosyl Residues

et al. 2001

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Surfactant protein D (SP-D), a C-type lectin, is an important pulmonary host defense molecule. Carbohydrate binding is critical to its host defense properties, but the precise polysaccharide structures recognized by the protein are unknown. SP-D binding toAspergillus fumigatus is strongly inhibited by a soluble β-(1→6)-linked but not by a soluble β-(1→3)-linked glucosyl homopolysaccharide (pustulan and laminarin, respectively), suggesting that SP-D recognizes only certain polysaccharide configurations, likely through differential binding to nonterminal glucosyl residues. In this study we have computationally docked α/β-dglucopyranose and α/β-(1→2)-, α/β-(1→3)-, α/β-(1→4)-, and α/β-(1→6)-linked glucosyl trisaccharides into the SP-D carbohydrate recognition domain. As with the mannose-binding proteins, we found significant hydrogen bonding between the protein and the vicinal, equatorial OH groups at the 3 and 4 positions on the sugar ring. Our docking studies predict that α/β-(1→2)-, α-(1→4)-, and α/β-(1→6)-linked but not α/β-(1→3)-linked glucosyl trisaccharides can be bound by their internal glucosyl residues and that binding also occurs through interactions of the protein with the 2-and 3-equatorial OH groups on the glucosyl ring. By using various soluble glucosyl homopolysaccharides as inhibitors of SP-D carbohydrate binding, we confirmed the interactions predicted by our modeling studies. Given the sequence and structural similarity between SP-D and other C-type lectins, many of the predicted interactions should be applicable to this protein family. Disciplines Biochemical and Biomolecular Engineering | Biological Engineering | Chemical Engineering CommentsThis work was supported by grants from NIH (HL-29891) and EPA (R825702 ABSTRACT: Surfactant protein D (SP-D), a C-type lectin, is an important pulmonary host defense molecule. Carbohydrate binding is critical to its host defense properties, but the precise polysaccharide structures recognized by the protein are unknown. SP-D binding to Aspergillus fumigatus is strongly inhibited by a soluble -(1f6)-linked but not by a soluble -(1f3)-linked glucosyl homopolysaccharide (pustulan and laminarin, respectively), suggesting that SP-D recognizes only certain polysaccharide configurations, likely through differential binding to nonterminal glucosyl residues. In this study we have computationally docked R/ -D-glucopyranose and R/ -(1f2)-, R/ -(1f3)-, R/ -(1f4)-, and R/ -(1f6)-linked glucosyl trisaccharides into the SP-D carbohydrate recognition domain. As with the mannose-binding proteins, we found significant hydrogen bonding between the protein and the vicinal, equatorial OH groups at the 3 and 4 positions on the sugar ring. Our docking studies predict that R/ -(1f2)-, R-(1f4)-, and R/ -(1f6)-linked but not R/ -(1f3)-linked glucosyl trisaccharides can be bound by their internal glucosyl residues and that binding also occurs through interactions of the protein with the 2-and 3-equatorial OH groups on the glucosyl ring. By using various soluble glucosyl homopo...

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Section: Discussionsupporting

confidence: 62%

“…Several structures of MBP complexed with carbohydrate ligands have been reported (11,12). On the basis of these …”

Section: Resultsmentioning

confidence: 99%

Section: Docking Of Glucose Into Sp-dmentioning

confidence: 90%

Section: Discussionmentioning

confidence: 99%

Section: Sp-d Binds Many Microorganisms In Vitromentioning

confidence: 96%

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Polysaccharide Recognition by Surfactant Protein D: Novel Interactions of a C-Type Lectin with Nonterminal Glucosyl Residues

et al. 2001

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Molecular organization, structural features, and ligand binding characteristics of CD44, a highly variable cell surface glycoprotein with multiple functions

Bajorath

2000

Proteins

141

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CD44 is a type I transmembrane protein and member of the cartilage link protein family. It is involved in cell-cell and cell-matrix interactions and signal transduction. Several CD44 ligands have been identified. CD44 is a major cell surface receptor for hyaluronan, a component of the extracellular matrix. It is implicated in diseases such as cancer and inflammation and therefore intensely studied. A characteristic feature of CD44 is the occurrence of many isoforms that are expressed in a cell-specific manner and differentially glycosylated. Although a number of CD44 isoforms have been characterized, the structural diversity of CD44 makes it often challenging to study (isoform-specific) CD44-ligand interactions at the molecular level of detail. The structural organization and ligand binding characteristics of CD44 are focal points of this review. On the basis of recent structural and mutagenesis studies, details of the CD44-hyaluronan interaction are beginning to be understood. Proteins 2000;39:103-111.

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Design, synthesis and characterisation of affinity ligands for glycoproteins

et al. 1999

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The concepts of rational design and solid phase combinatorial chemistry were used to develop affinity adsorbents for glycoproteins. A detailed assessment of protein-carbohydrate interactions was used to identify key residues that determine monosaccharide specificity, which were subsequently exploited as the basis for the synthesis of a library of glycoprotein binding ligands. The ligands were synthesised using solid phase combinatorial chemistry and were assessed for their sugar-binding ability with the glycoenzymes, glucose oxidase and RNase B. Partial and completely deglycosylated enzymes were used as controls. The triazine-based ligand, histamine/tryptamine (8/10) was identified as a putative glycoprotein binding ligand, since it displayed particular affinity for glucose oxidase and other mannosylated glycoproteins. Experiments with deglycosylated control proteins, specific eluants and retardation in the presence of competing sugars strongly suggest that the ligand binds the carbohydrate moiety of glucose oxidase rather than the protein itself.

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Structure of a C-type mannose-binding protein complexed with an oligosaccharide

Cited by 899 publications

References 47 publications

Polysaccharide Recognition by Surfactant Protein D: Novel Interactions of a C-Type Lectin with Nonterminal Glucosyl Residues

Polysaccharide Recognition by Surfactant Protein D: Novel Interactions of a C-Type Lectin with Nonterminal Glucosyl Residues

Molecular organization, structural features, and ligand binding characteristics of CD44, a highly variable cell surface glycoprotein with multiple functions

Design, synthesis and characterisation of affinity ligands for glycoproteins

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