| Structure and binding analysis of Polyporus squamosus lectin in complex with the Neu5Ac{alpha}2-6Gal{beta}1-4GlcNAc human-type influenza receptor. | |
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MedLine Citation:
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PMID: 21436237 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Glycan chains that terminate in sialic acid (Neu5Ac) are frequently the receptors targeted by pathogens for initial adhesion. Carbohydrate-binding proteins (lectins) with specificity for Neu5Ac are particularly useful in the detection and isolation of sialylated glycoconjugates, such as those associated with pathogen adhesion as well as those characteristic of several diseases including cancer. Structural studies of lectins are essential in order to understand the origin of their specificity, which is particularly important when employing such reagents as diagnostic tools. Here, we report a crystallographic and molecular dynamics (MD) analysis of a lectin from Polyporus squamosus (PSL) that is specific for glycans terminating with the sequence Neu5Acα2-6Galβ. Because of its importance as a histological reagent, the PSL structure was solved (to 1.7 Å) in complex with a trisaccharide, whose sequence (Neu5Acα2-6Galβ1-4GlcNAc) is exploited by influenza A hemagglutinin for viral adhesion to human tissue. The structural data illuminate the origin of the high specificity of PSL for the Neu5Acα2-6Gal sequence. Theoretical binding free energies derived from the MD data confirm the key interactions identified crystallographically and provide additional insight into the relative contributions from each amino acid, as well as estimates of the importance of entropic and enthalpic contributions to binding. |
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Authors:
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Renuka Kadirvelraj; Oliver C Grant; Irwin J Goldstein; Harry C Winter; Hiroaki Tateno; Elisa Fadda; Robert J Woods |
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Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't Date: 2011-03-24 |
Journal Detail:
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Title: Glycobiology Volume: 21 ISSN: 1460-2423 ISO Abbreviation: Glycobiology Publication Date: 2011 Jul |
Date Detail:
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Created Date: 2011-06-09 Completed Date: 2011-10-03 Revised Date: 2012-09-24 |
Medline Journal Info:
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Nlm Unique ID: 9104124 Medline TA: Glycobiology Country: England |
Other Details:
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Languages: eng Pagination: 973-84 Citation Subset: IM |
Affiliation:
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Complex Carbohydrate Research Center, University of Georgia, Athens, GA 30602, USA. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Cell Adhesion Computer Simulation Crystallography, X-Ray Glycoconjugates Hemagglutinin Glycoproteins, Influenza Virus / metabolism Humans Lectins / chemistry*, metabolism* N-Acetylneuraminic Acid / metabolism* Polyporus / metabolism* Receptors, Cell Surface Trisaccharides / chemistry, metabolism* |
| Grant Support | |
ID/Acronym/Agency:
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GM055230/GM/NIGMS NIH HHS; GM094919/GM/NIGMS NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Glycoconjugates; 0/Hemagglutinin Glycoproteins, Influenza Virus; 0/Lectins; 0/Receptors, Cell Surface; 0/Trisaccharides; 0/saccharide-binding proteins; 131-48-6/N-Acetylneuraminic Acid |
| Comments/Corrections | |
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