Computational Studies on PA-IIL Lectin-Carbohydrate Interactions

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F07%3A00020642" target="_blank" >RIV/00216224:14310/07:00020642 - isvavai.cz</a>

Výsledek na webu

—

DOI - Digital Object Identifier

—

Jazyk výsledku

angličtina

Název v původním jazyce

Computational Studies on PA-IIL Lectin-Carbohydrate Interactions

Popis výsledku v původním jazyce

Lectins are proteins of nonimmune origin that non-enzymatically selectively bind to mono or oligosaccharides. Multifarious activity of carbohydrates in biophysiological pathway, such as immune activity, tumor metastasis, cell-cell recognition, bacterialpathogenecity, open an avenue for the lectin-carbohydrate interaction research, which is also a big challenge for theoretical modeling due to the polar flexible saccharide moiety. One of the lectins, PA-IIL that produced by Pseudomonas aeruginosa, whichplay significant role in cystic fibrosis disease, motivated our study on PA-IIL-carbohydrate interactions. The structure can provide a static view of the macromolecules, but for the full understanding of protein-ligand interactions it is necessary to know all the accessible spatial orientations of the ligand in the receptor binding pocket.

Název v anglickém jazyce

Computational Studies on PA-IIL Lectin-Carbohydrate Interactions

Popis výsledku anglicky

Lectins are proteins of nonimmune origin that non-enzymatically selectively bind to mono or oligosaccharides. Multifarious activity of carbohydrates in biophysiological pathway, such as immune activity, tumor metastasis, cell-cell recognition, bacterialpathogenecity, open an avenue for the lectin-carbohydrate interaction research, which is also a big challenge for theoretical modeling due to the polar flexible saccharide moiety. One of the lectins, PA-IIL that produced by Pseudomonas aeruginosa, whichplay significant role in cystic fibrosis disease, motivated our study on PA-IIL-carbohydrate interactions. The structure can provide a static view of the macromolecules, but for the full understanding of protein-ligand interactions it is necessary to know all the accessible spatial orientations of the ligand in the receptor binding pocket.

Druh

O - Ostatní výsledky

CEP obor

CE - Biochemie

OECD FORD obor

—

Projekt

<a href="/cs/project/GD204%2F03%2FH016" target="_blank" >GD204/03/H016: Strukturní biofyzika makromolekul</a><br>

Návaznosti

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

Rok uplatnění

2007

Kód důvěrnosti údajů

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