A point mutation led to overturn in sugar-binding specificity of lectin RS-IIL from PA-IIL lectin superfamily

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F15%3A00081460" target="_blank" >RIV/00216224:14310/15:00081460 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

A point mutation led to overturn in sugar-binding specificity of lectin RS-IIL from PA-IIL lectin superfamily

Popis výsledku v původním jazyce

The so-called ?PA-IIL lectin superfamily? includes several lectins from human opportunistic pathogens: PA-IIL (from Pseudomonas aeruginosa), CV-IIL (from Chromobacterium violaceum), BC2L-A and C-terminal domain from BC2L-C (from Burkholderia cenocepacia). Also, it includes one lectin from important plant pathogen: RS-IIL (from Ralstonia solanacearum). All these lectins are homologues with significant sequential and structural similarities but they differ in sugar-binding specificity. This fact is causedby differences in three amino acids which are arranged in the so-called ?specificity binding loop? (amino acids at positions 22-23-24). The previous study, which was focused on investigation of fine specificity of PA-IIL, confirmed that amino acid at position 22 is mainly responsible for sugar binding specificity. Specific amino acid substitution in this position led to change of sugar preference of PA-IIL to the RS-IIL one.

Název v anglickém jazyce

A point mutation led to overturn in sugar-binding specificity of lectin RS-IIL from PA-IIL lectin superfamily

Popis výsledku anglicky

The so-called ?PA-IIL lectin superfamily? includes several lectins from human opportunistic pathogens: PA-IIL (from Pseudomonas aeruginosa), CV-IIL (from Chromobacterium violaceum), BC2L-A and C-terminal domain from BC2L-C (from Burkholderia cenocepacia). Also, it includes one lectin from important plant pathogen: RS-IIL (from Ralstonia solanacearum). All these lectins are homologues with significant sequential and structural similarities but they differ in sugar-binding specificity. This fact is causedby differences in three amino acids which are arranged in the so-called ?specificity binding loop? (amino acids at positions 22-23-24). The previous study, which was focused on investigation of fine specificity of PA-IIL, confirmed that amino acid at position 22 is mainly responsible for sugar binding specificity. Specific amino acid substitution in this position led to change of sugar preference of PA-IIL to the RS-IIL one.

Druh

O - Ostatní výsledky

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2015

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů