Structural and functional determination of predicted core fucose specific mutants of Ralstonia solanacearum lectin

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F16%3A00088252" target="_blank" >RIV/00216224:14310/16:00088252 - isvavai.cz</a>
Result on the web
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DOI - Digital Object Identifier
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Result language
angličtina
Original language name
Structural and functional determination of predicted core fucose specific mutants of Ralstonia solanacearum lectin
Original language description
Lectins (from Latin, legere, to select or choose) are multivalent proteins with the ability to recognize and reversibly bind mono- and oligosacharides. The sugar binding sites of lectins, called carbohydrate recognition domain (CRD), promote specific recognition in accordance with the key-lock model. Mutagenesis in CRD may lead to the improvement of binding specificity of lectins, making them markers for carbohydrate structural motifs in nature. Ralstonia solanacearum lectin (RSL) isolated from Ralstonia solanacearum, a phytopathogen causing lethal wilting of agricultural crops, is a trimeric L-fucose specific lectin with the six bladed b-propeller fold. Each monomer presents two fucose specific binding sites, resulting in six symmetrically arranged CRDs. Core fucosylation is the most important core modification in vertebrate N-glycans. It is the addition of fucose via a1-6 linkage to the N-acetylglucosamine adjecent to asparagine in the core.
Czech name
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Czech description
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Project
<a href="/en/project/GA13-25401S" target="_blank" >GA13-25401S: Study of proteins from pathogens involved in host organism recognition</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year
2016
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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