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Computational Studies on PA-IIL Lectin-Carbohydrate Interactions

The result's identifiers

  • Result code in 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>

  • Result on the web

  • DOI - Digital Object Identifier

Alternative languages

  • Result language

    angličtina

  • Original language name

    Computational Studies on PA-IIL Lectin-Carbohydrate Interactions

  • Original language description

    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.

  • Czech name

  • Czech description

Classification

  • Type

    O - Miscellaneous

  • CEP classification

    CE - Biochemistry

  • OECD FORD branch

Result continuities

  • Project

    <a href="/en/project/GD204%2F03%2FH016" target="_blank" >GD204/03/H016: Structural biophysics of macromolecules</a><br>

  • Continuities

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

Others

  • Publication year

    2007

  • Confidentiality

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