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• W1966593497 abstract "Art v 1 is the major allergen of mugwort (Artemisia vulgaris) pollen. It is formed by an N-terminal globular defensin-like part and a C-terminal proline-rich domain. As the structure and the dynamics of Art v 1 have been mostly described for its recombinant, non-glycosylated form, which does not occur in normal plant physiology, the present work intends to obtain a three-dimensional model for Art v 1 native O-glycosylation structure and to evaluate the influence of such glycans over the protein dynamics and allergenicity through molecular dynamics simulations in triplicates. Structural insights into the mutual recognition of Art v 1 protein and carbohydrate moieties recognition by antibodies were obtained, in which glycan chains remained close to the previously identified epitopes in the defensin-like domain, thus pointing to potential interferences with antibodies recognition. To our knowledge, this is the first structural report of an entire furanose-containing glycoprotein. As well, together with the previously determined NMR structures, the obtained results contribute in the comprehension of the effect of glycosylation over both proline-rich and defensin-like domains, providing an atomic representation of such alterations." @default.
• W1966593497 created "2016-06-24" @default.
• W1966593497 creator A5032190365 @default.
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• W1966593497 date "2012-02-23" @default.
• W1966593497 modified "2023-09-27" @default.
• W1966593497 title "Structural glycobiology of the major allergen of Artemisia vulgaris pollen, Art v 1: O-glycosylation influence on the protein dynamics and allergenicity" @default.
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• W1966593497 doi "https://doi.org/10.1093/glycob/cws056" @default.
• W1966593497 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/22367746" @default.
• W1966593497 hasPublicationYear "2012" @default.
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